2jpn

Solution Structure of T4 Bacteriophage Helicase Uvsw.1

spinqualitylabelsall models 2jpn Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2jpn is a 1 chain structure with sequence from Escherichia virus T4. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function UVSW_BPT4 DNA helicase that catalyzes branch migration and dissociation of RNA-DNA hybrids. Plays a critical role in a specific recombination pathway involving simple reciprocal exchange. UvsW protein is normally the key regulatory factor in the switch from early to late phage DNA replication. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The uvsWXY system is implicated in the replication and repair of the bacteriophage T4 genome. Whereas the roles of the recombinase (UvsX) and the recombination mediator protein (UvsY) are known, the precise role of UvsW is unclear. Sequence analysis identifies UvsW as a member of the monomeric SF2 helicase superfamily that translocates nucleic acid substrates via the action of two RecA-like motor domains. Functional homologies to Escherichia coli RecG and biochemical analyses have shown that UvsW interacts with branched nucleic acid substrates, suggesting roles in recombination and the rescue of stalled replication forks. A sequencing error at the 3'-end of the uvsW gene has revealed a second, short open reading frame that encodes a protein of unknown function called UvsW.1. We have determined the crystal structure of UvsW to 2.7A and the NMR solution structure of UvsW.1. UvsW has a four-domain architecture with structural homology to the eukaryotic SF2 helicase, Rad54. A model of the UvsW-ssDNA complex identifies structural elements and conserved residues that may interact with nucleic acid substrates. The NMR solution structure of UvsW.1 reveals a dynamic four-helix bundle with homology to the structure-specific nucleic acid binding module of RecQ helicases. Crystallographic and NMR analyses of UvsW and UvsW.1 from bacteriophage T4.,Kerr ID, Sivakolundu S, Li Z, Buchsbaum JC, Knox LA, Kriwacki R, White SW J Biol Chem. 2007 Nov 23;282(47):34392-400. Epub 2007 Sep 17. PMID:17878153 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Helicase 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA