Viser treff 448-467 av 527

    • Strong Duschinsky Mixing Induced Breakdown of Kasha's Rule in an Organic Phosphor 

      Paul, Lopa; Moitra, Torsha; Ruud, Kenneth; Chakrabarti, Swapan (Journal article; Tidsskriftartikkel; Peer reviewed, 2019-01-08)
      We present the novel observation that Duschinsky mixings can lead to the breakdown of Kasha’s rule in a white light phosphor molecule, dibenzo[<i>b,d</i>]thiophen-2-yl (4-chlorophenyl)methanone. Our theoretical analyses show the energy gap between the T<sub>1</sub> and T<sub>2</sub> states (0.48 eV) is too large to allow for any significant population of the T<sub>2</sub> state at room temperature ...
    • Structural and biochemical characterization of the environmental MBLs MYO-1, ECV-1 and SHD-1 

      Frøhlich, Christopher; Sørum, Vidar; Huber, Sandra; Samuelsen, Ørjan; Berglund, Fanny; Kristiansson, Erik; Kotsakis, Stathis D.; Marathe, Nachiket P.; Larsson, Joakim; Leiros, Hanna-Kirsti S. (Journal article; Tidsskriftartikkel; Peer reviewed, 2020-05-28)
      <i>Background</i> - MBLs form a large and heterogeneous group of bacterial enzymes conferring resistance to β-lactam antibiotics, including carbapenems. A large environmental reservoir of MBLs has been identified, which can act as a source for transfer into human pathogens. Therefore, structural investigation of environmental and clinically rare MBLs can give new insights into structure–activity ...
    • Structural and biochemical characterization of the environmental MBLs MYO-1, ECV-1 and SHD-1 

      Frøhlich, Christopher; Sørum, Vidar; Huber, Sandra; Samuelsen, Ørjan; Berglund, Fanny; Kristiansson, Erik; Kotsakis, Stathis D.; Marathe, Nachiket; Larsson, DG Joakim; Leiros, Hanna-Kirsti Schrøder (Journal article; Tidsskriftartikkel; Peer reviewed, 2020-05-28)
      Background: MBLs form a large and heterogeneous group of bacterial enzymes conferring resistance to b-lactam antibiotics, including carbapenems. A large environmental reservoir of MBLs has been identified, which can act as a source for transfer into human pathogens. Therefore, structural investigation of environmental and clinically rare MBLs can give new insights into structure–activity relationships ...
    • Structural and biochemical characterization of VIM-26 shows that Leu224 has implications for the substrate specificity of VIM metallo-β-lactamases 

      Leiros, Hanna-Kirsti S.; Edvardsen, Kine Susann Waade; Bjerga, Gro Elin Kjæreng; Samuelsen, Ørjan (Journal article; Tidsskriftartikkel; Peer reviewed, 2015-02-06)
      During the last decades antimicrobial resistance has become a global health problem. Metallo-β-lactamases (MBLs) which are broad-spectrum β-lactamases that inactivate virtually all β-lactams including carbapenems, are contributing to this health problem. In this study a novel MBL variant, termed VIM-26, identified in a Klebsiella pneumoniae isolate was studied. VIM-26 belongs to the Verona ...
    • Structural and biophysical analysis of interactions between cod and human uracil-DNA N-glycosylase (UNG) and UNG inhibitor (Ugi) 

      Assefa, Netsanet Gizaw; Niiranen, Laila; Johnson, Kenneth; Leiros, Hanna-Kirsti S.; Smalås, Arne O.; Willassen, Nils Peder; Moe, Elin (Journal article; Tidsskriftartikkel; Peer reviewed, 2014-07-25)
      Uracil-DNA N-glycosylase from Atlantic cod (cUNG) shows cold-adapted features such as high catalytic efficiency, a low temperature optimum for activity and reduced thermal stability compared with its mesophilic homologue human UNG (hUNG). In order to understand the role of the enzyme–substrate interaction related to the cold-adapted properties, the structure of cUNG in complex with a bacteriophage ...
    • Structural and functional variation of chitin-binding domains of a lytic polysaccharide monooxygenase from Cellvibrio japonicus 

      Madland, Eva; Forsberg, Zarah; Wang, Yong; Lindorff-Larsen, Kresten; Niebisch, Axel; Modregger, Jan; Eijsink, Vincent; Aachmann, Finn Lillelund; Courtade, Gaston (Journal article; Tidsskriftartikkel; Peer reviewed, 2021-08-17)
      Among the extensive repertoire of carbohydrate-active enzymes, lytic polysaccharide monooxygenases (LPMOs) have a key role in recalcitrant biomass degradation. LPMOs are copper-dependent enzymes that catalyze oxidative cleavage of glycosidic bonds in polysaccharides such as cellulose and chitin. Several LPMOs contain carbohydrate-binding modules (CBMs) that are known to promote LPMO efficiency. ...
    • Structural and thermodynamic insight into phenylalanine hydroxylase from the human pathogen Legionella pneumophila 

      Leiros, Hanna-Kirsti S.; Flydal, Marte Innselset; Martinez, Aurora (Journal article; Tidsskriftartikkel; Peer reviewed, 2013)
      Phenylalanine hydroxylase from Legionella pneumophila (lpPAH) has a major functional role in the synthesis of the pigment pyomelanin, which is a potential virulence factor. We present here the crystal structure of lpPAH, which is a dimeric enzyme that shows high thermostability, with a midpoint denat- uration temperature of 79 ◦C, and low substrate affinity. The structure revealed a dimerization ...
    • Structural insight into a CE15 esterase from the marine bacterial metagenome 

      De Santi, Concetta; Gani, Osman A. B. S. M.; Helland, Ronny; Williamson, Adele Kim (Journal article; Tidsskriftartikkel; Peer reviewed, 2017-12-08)
      The family 15 carbohydrate esterase (CE15) MZ0003, which derives from a marine Arctic metagenome, has a broader substrate scope than other members of this family. Here we report the crystal structure of MZ0003, which reveals that residues comprising the catalytic triad differ from previously-characterized fungal homologs, and resolves three large loop regions that are unique to this bacterial ...
    • Structural insight into DNA joining: from conserved mechanisms to diverse scaffolds 

      Williamson, Adele Kim; Leiros, Hanna-Kirsti S. (Journal article; Tidsskriftartikkel; Peer reviewed, 2020-05-04)
      DNA ligases are diverse enzymes with essential functions in replication and repair of DNA; here we review recent advances in their structure and distribution and discuss how this contributes to understanding their biological roles and technological potential. Recent high-resolution crystal structures of DNA ligases from different organisms, including DNA-bound states and reaction intermediates, have ...
    • Structural insight into DNA joining: from conserved mechanisms to diverse scaffolds 

      Williamson, Adele Kim; Leiros, Hanna-Kirsti S. (Journal article; Tidsskriftartikkel; Peer reviewed, 2020-05-04)
      DNA ligases are diverse enzymes with essential functions in replication and repair of DNA; here we review recent advances in their structure and distribution and discuss how this contributes to understanding their biological roles and technological potential. Recent high-resolution crystal structures of DNA ligases from different organisms, including DNA-bound states and reaction intermediates, have ...
    • Structural insights into the enhanced carbapenemase efficiency of OXA-655 compared to OXA-10 

      Leiros, Hanna-Kirsti S.; Thomassen, Ane Molden; Samuelsen, Ørjan; Flach, Carl-Fredrik; Kotsakis, Stathis D.; Larsson, Joakim (Journal article; Tidsskriftartikkel; Peer reviewed, 2020-07-19)
      Carbapenemases are the main cause of carbapenem resistance in Gram‐negative bacteria. How β‐lactamases with weak carbapenemase activity, such as the OXA‐10‐type class D β‐lactamases, contribute to anti‐bacterial drug resistance is unclear. OXA‐655 is a T26M and V117L OXA‐10 variant, recently identified from hospital wastewater. Despite exhibiting stronger carbapenemase activity towards ertapenem ...
    • Structural insights into TMB-1 and the role of residues 119 and 228 in substrate and inhibitor binding 

      Skagseth, Susann; Christopeit, Tony; Akhter, Sundus; Bayer, Annette; Samuelsen, Ørjan; Leiros, Hanna-Kirsti S. (Journal article; Tidsskriftartikkel; Peer reviewed, 2017-05-30)
      Metallo-β-lactamases (MBLs) threaten the effectiveness of β-lactam antibiotics, including carbapenems, and are a concern for global public health. β-Lactam/β-lactamase inhibitor combinations active against class A and class D carbapenemases are used, but no clinically useful MBL inhibitor is currently available. Tripoli metallo-β-lactamase-1 (TMB-1) and TMB-2 are members of MBL subclass B1a, where ...
    • Structural insights of the enzymes from the chitin utilization locus of Flavobacterium johnsoniae 

      Mazurkewich, Scott; Helland, Ronny; Mackenzie, Alasdair; Eijsink, Vincent; Pope, Phillip Byron; Brändén, Gisela; Larsbrink, Johan (Journal article; Tidsskriftartikkel; Peer reviewed, 2020-08-13)
      Chitin is one of the most abundant renewable organic materials found on earth. The chitin utilization locus in <i>Flavobacterium johnsoniae</i>, which encodes necessary proteins for complete enzymatic depolymerization of crystalline chitin, has recently been characterized but no detailed structural information on the enzymes was provided. Here we present protein structures of the <i>F. johnsoniae</i> ...
    • Structural intermediates of a DNA-ligase complex illuminate the role of the catalytic metal ion and mechanism of phosphodiester bond formation 

      Williamson, Adele Kim; Leiros, Hanna-Kirsti S. (Journal article; Tidsskriftartikkel; Peer reviewed, 2019-07-17)
      DNA ligases join adjacent 5′ phosphate (5′P) and 3′ hydroxyl (3′OH) termini of double-stranded DNA via a three-step mechanism requiring a nucleotide cofactor and divalent metal ion. Although considerable structural detail is available for the first two steps, less is known about step 3 where the DNA-backbone is joined or about the cation role at this step. We have captured high-resolution structures ...
    • Structural Organization of S516 Group I Introns in Myxomycetes 

      Furulund, Betty Martine Normann; Karlsen, Bård Ove; Babiak, Igor; Haugen, Peik; Johansen, Steinar Daae (Journal article; Tidsskriftartikkel; Peer reviewed, 2022-05-25)
      Group I introns are mobile genetic elements encoding self-splicing ribozymes. Group I introns in nuclear genes are restricted to ribosomal DNA of eukaryotic microorganisms. For example, the myxomycetes, which represent a distinct protist phylum with a unique life strategy, are rich in nucleolar group I introns. We analyzed and compared 75 group I introns at position 516 in the small subunit ...
    • Structural studies of triazole inhibitors with promising inhibitor effects against antibiotic resistance metallo-β-lactamases 

      Muhammad, Zeeshan; Skagseth, Susann; Boomgaren, Marc; Akhter, Sundus; Frøhlich, Christopher; Ismael, Aya; Christopeit, Tony; Bayer, Annette; Leiros, Hanna-Kirsti S. (Journal article; Tidsskriftartikkel; Peer reviewed, 2020-06-18)
      Metallo-β-lactamases (MBLs) are an emerging cause of bacterial antibiotic resistance by hydrolysing all classes of β-lactams except monobactams, and the MBLs are not inhibited by clinically available serine-β-lactamase inhibitors. Two of the most commonly encountered MBLs in clinical isolates worldwide – the New Delhi metallo-β-lactamase (NDM-1) and the Verona integron-encoded metallo-β-lactamase ...
    • Structure and function of a CE4 deacetylase isolated from a marine environment 

      Tuveng, Tina Rise; Rothweiler, Ulli; Udatha, D.B.R.K. Gupta; Vaaje-Kolstad, Gustav; Smalås, Arne O.; Eijsink, Vincent (Journal article; Tidsskriftartikkel; Peer reviewed, 2017-11-06)
      Chitin, a polymer of β(1–4)-linked N-acetylglucosamine found in e.g. arthropods, is a valuable resource that may be used to produce chitosan and chitooligosaccharides, two compounds with considerable industrial and biomedical potential. Deacetylating enzymes may be used to tailor the properties of chitin and its derived products. Here, we describe a novel CE4 enzyme originating from a marine ...
    • Structure and Mechanism of a Cold-Adapted Bacterial Lipase 

      van der Ent, Florian; Lund, Bjarte Aarmo; Svalberg, Linn; Purg, Miha; Chukwu, Ghislean; Widersten, Mikael; Isaksen, Geir Villy; Brandsdal, Bjørn Olav; Åqvist, Johan Lennart Gösta (Journal article; Tidsskriftartikkel; Peer reviewed, 2022-05-03)
      The structural origin of enzyme cold-adaptation has been the subject of considerable research efforts in recent years. Comparative studies of orthologous mesophilic–psychrophilic enzyme pairs found in nature are an obvious strategy for solving this problem, but they often suffer from relatively low sequence identity of the enzyme pairs. Small bacterial lipases adapted to distinctly different ...
    • Structure and mechanism of a phage-encoded SAM lyase revises catalytic function of enzyme family 

      Isaksen, Geir Villy; Guo, Xiaohu; Söderholm, Annika; Kanchugal P, Sandesh; Warsi, Omar; Eckhard, Ulrich; Silvia, Trigüis; Gogoll, Adolf; Jerlström-Hultqvist, Jon; Åqvist, Johan; Anderson, Dan I; Selmer, Maria (Journal article; Tidsskriftartikkel; Peer reviewed, 2021-02-10)
      The first S-adenosyl methionine (SAM) degrading enzyme (SAMase) was discovered in bacteriophage T3, as a counter-defense against the bacterial restriction-modification system, and annotated as a SAM hydrolase forming 5’ methyl-thioadenosine (MTA) and L-homoserine. From environmental phages, we recently discovered three SAMases with barely detectable sequence similarity to T3 SAMase and without ...
    • Structure determination of uracil-DNA N-glycosylase from Deinococcus radiodurans in complex with DNA 

      Pedersen, Hege Lynum; Johnson, Kenneth; McVey, Colin; Leiros, Ingar; Moe, Elin (Journal article; Tidsskriftartikkel; Peer reviewed, 2015-10-01)