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dc.contributor.authorWilliamson, Adele Kim
dc.contributor.authorRothweiler, Ulli
dc.contributor.authorLeiros, Hanna-Kirsti S.
dc.date.accessioned2016-03-14T08:35:50Z
dc.date.available2016-03-14T08:35:50Z
dc.date.issued2014-11-01
dc.description.abstractDNA ligases are a structurally diverse class of enzymes which share a common catalytic core and seal breaks in the phosphodiester backbone of double-stranded DNA via an adenylated intermediate. Here, the structure and activity of a recombinantly produced ATP-dependent DNA ligase from the bacterium Psychromonas sp. strain SP041 is described. This minimal-type ligase, like its close homologues, is able to ligate singly nicked double-stranded DNA with high efficiency and to join cohesive-ended and blunt-ended substrates to a more limited extent. The 1.65 A˚ resolution crystal structure of the enzyme–adenylate complex reveals no unstructured loops or segments, and suggests that this enzyme binds the DNA without requiring full encirclement of the DNA duplex. This is in contrast to previously characterized minimal DNA ligases from viruses, which use flexible loop regions for DNA interaction. The Psychromonas sp. enzyme is the first structure available for the minimal type of bacterial DNA ligases and is the smallest DNA ligase to be crystallized to date.en_US
dc.descriptionPublished version also available at <a href=http://dx.doi.org/10.1107/S1399004714021099>http://dx.doi.org/10.1107/S1399004714021099</a>en_US
dc.identifier.citationActa Crystallographica Section D: Biological Crystallography 2014, 70(11):3043-3056en_US
dc.identifier.cristinIDFRIDAID 1205906
dc.identifier.doi10.1107/S1399004714021099
dc.identifier.issn0907-4449
dc.identifier.urihttps://hdl.handle.net/10037/8913
dc.identifier.urnURN:NBN:no-uit_munin_8509
dc.language.isoengen_US
dc.publisherInternational Union of Crystallographyen_US
dc.relation.projectIDNorges forskningsråd: 192123
dc.rights.accessRightsopenAccess
dc.subjectVDP::Matematikk og Naturvitenskap: 400::Kjemi: 440en_US
dc.subjectVDP::Mathematics and natural science: 400::Chemistry: 440en_US
dc.titleEnzyme-adenylate structure of a bacterial ATP-dependent DNA ligase with a minimized DNA-binding surfaceen_US
dc.typeJournal articleen_US
dc.typeTidsskriftartikkelen_US
dc.typePeer revieweden_US


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