1wp9
From Proteopedia
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Crystal structure of Pyrococcus furiosus Hef helicase domain
Overview
DNA and RNA frequently form various branched intermediates that are, important for the transmission of genetic information. Helicases play, pivotal roles in the processing of these transient intermediates during, nucleic acid metabolism. The archaeal Hef helicase/ nuclease is a, representative protein that processes flap- or fork-DNA structures, and, intriguingly, its C-terminal half belongs to the XPF/Mus81 nuclease, family. Here, we report the crystal structure of the helicase domain of, the Hef protein from Pyrococcus furiosus. The structure reveals a novel, helical insertion between the two conserved helicase core domains. This, positively charged extra region, structurally similar to the "thumb", domain of DNA polymerase, plays critical roles in fork recognition. The, Hef helicase/nuclease exhibits sequence similarity to the Mph1 helicase, from Saccharomyces cerevisiae; XPF/Rad1, involved in DNA repair; and a, putative Hef homolog identified in mammals. Hence, our findings provide a, structural basis for the functional mechanisms of this helicase/nuclease, family.
About this Structure
1WP9 is a Single protein structure of sequence from Pyrococcus furiosus dsm 3638 with PO4 as ligand. Active as Adenosinetriphosphatase, with EC number 3.6.1.3 Full crystallographic information is available from OCA.
Reference
Crystal structure and functional implications of Pyrococcus furiosus hef helicase domain involved in branched DNA processing., Nishino T, Komori K, Tsuchiya D, Ishino Y, Morikawa K, Structure. 2005 Jan;13(1):143-53. PMID:15642269
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