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PDBsum entry 4d05
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References listed in PDB file
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Key reference
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Title
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Enzyme-Adenylate structure of a bacterial ATP-Dependent DNA ligase with a minimized DNA-Binding surface.
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Authors
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A.Williamson,
U.Rothweiler,
H.K.Leiros.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2014,
70,
3043-3056.
[DOI no: ]
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PubMed id
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Abstract
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DNA 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 Å 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.
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