1WP9

Crystal structure of Pyrococcus furiosus Hef helicase domain

Summary for 1WP9

• Entry DOI: 10.2210/pdb1wp9/pdb
• Related: 1j22 1j23 1j24 1j25
• Descriptor: ATP-dependent RNA helicase, putative, PHOSPHATE ION (3 entities in total)
• Functional Keywords: helicase, atpase, dna replication, dna repair, dna recombination, hydrolase
• Biological source: Pyrococcus furiosus
• Total number of polymer chains: 6
• Total formula weight: 338595.97

Authors

Nishino, T.,Komori, K.,Tsuchiya, D.,Ishino, Y.,Morikawa, K. (deposition date: 2004-08-31, release date: 2005-02-01, Last modification date: 2024-05-29)

Primary citation

Nishino, T.,Komori, K.,Tsuchiya, D.,Ishino, Y.,Morikawa, K.
Crystal Structure and Functional Implications of Pyrococcus furiosus Hef Helicase Domain Involved in Branched DNA Processing
Structure, 13:143-153, 2005

PubMed Abstract: 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.

PubMed: 15642269
DOI: 10.1016/j.str.2004.11.008

Experimental method

X-RAY DIFFRACTION (2.9 Å)