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'''Crystal Structure of human DNA polymerase lambda in complex with nicked DNA and pyrophosphate''' | '''Crystal Structure of human DNA polymerase lambda in complex with nicked DNA and pyrophosphate''' | ||
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[[Category: Kunkel, T A.]] | [[Category: Kunkel, T A.]] | ||
[[Category: Pedersen, L C.]] | [[Category: Pedersen, L C.]] | ||
[[Category: | [[Category: Dna polymerase lambda]] | ||
[[Category: | [[Category: Helix-hairpin-helix]] | ||
[[Category: | [[Category: Protein-dna complex]] | ||
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Revision as of 12:27, 3 May 2008
Crystal Structure of human DNA polymerase lambda in complex with nicked DNA and pyrophosphate
Overview
Pol lambda is a family X member believed to fill short gaps during DNA repair. Here we report crystal structures of Pol lambda representing three steps in filling a single-nucleotide gap. These structures indicate that, unlike other DNA polymerases, Pol lambda does not undergo large subdomain movements during catalysis, and they provide a clear characterization of the geometry and stereochemistry of the in-line nucleotidyl transfer reaction.
About this Structure
1XSP is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
A closed conformation for the Pol lambda catalytic cycle., Garcia-Diaz M, Bebenek K, Krahn JM, Kunkel TA, Pedersen LC, Nat Struct Mol Biol. 2005 Jan;12(1):97-8. Epub 2004 Dec 19. PMID:15608652 Page seeded by OCA on Sat May 3 15:27:46 2008