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2UUZ

Orthorhombic crystal form of GamS from bacteriophage lambda.

Summary for 2UUZ
Entry DOI10.2210/pdb2uuz/pdb
Related2UV1
DescriptorHOST-NUCLEASE INHIBITOR PROTEIN GAM (2 entities in total)
Functional Keywordsbacteriophage lambda, nuclease inhibitor, recbcd inhibitor, putative dna mimic, inhibitor
Biological sourceBACTERIOPHAGE LAMBDA
Total number of polymer chains2
Total formula weight23466.00
Authors
Court, R.I.,Cook, N.,Saikrishnan, K.,Wigley, D.B. (deposition date: 2007-03-08, release date: 2007-06-12, Last modification date: 2024-05-08)
Primary citationCourt, R.I.,Cook, N.,Saikrishnan, K.,Wigley, D.B.
The Crystal Structure of Lambda-Gam Protein Suggests a Model for Recbcd Inhibition.
J.Mol.Biol., 371:25-, 2007
Cited by
PubMed Abstract: In Escherichia coli, RecBCD processes double-stranded DNA breaks during the initial stages of homologous recombination. RecBCD contains helicase and nuclease activities, and unwinds and digests the blunt-ended DNA until a specific eight-nucleotide sequence, Chi, is encountered. Chi modulates the nuclease activity of RecBCD and results in a resected DNA end, which is a substrate for RecA during subsequent steps in recombination. RecBCD also acts as a defence mechanism against bacteriophage infection by digesting linear viral DNA present during virus replication or resulting from the action of restriction endonucleases. To avoid this fate, bacteriophage lambda encodes the gene Gam whose product is an inhibitor of RecBCD. Gam has been shown to bind to RecBCD and inhibit its helicase and nuclease activities. We show that Gam inhibits RecBCD by preventing it from binding DNA. We have solved the crystal structure of Gam from two different crystal forms. Using the published crystal structure of RecBCD in complex with DNA we suggest models for the molecular mechanism of Gam-mediated inhibition of RecBCD. We also propose that Gam could be a mimetic of single-stranded, and perhaps also double-stranded, DNA.
PubMed: 17544443
DOI: 10.1016/J.JMB.2007.05.037
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.3 Å)
Structure validation

245663

数据于2025-12-03公开中

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