3k70

Crystal structure of the complete initiation complex of RecBCD

spinqualitylabelsall models 3k70, resolution 3.59Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3k70 is a 8 chain structure with sequence from Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA NonStd Res: 5IU Related: 1w36 Gene: b2820, JW2788, recB, rorA (ECOLI), b2822, JW2790, recC (ECOLI), b2819, JW2787, recD (ECOLI) Activity: Exodeoxyribonuclease V, with EC number 3.1.11.5 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [EX5B_ECOLI] Required for efficient DNA repair; it catalyzes the unwinding of double-stranded DNA and the cleavage of single-stranded DNA and it stimulates local genetic recombination. All of these activities require concomitant hydrolysis of ATP. [EX5A_ECOLI] Exhibits several catalytic activities, including ATP-dependent exonuclease, ATP-stimulated endonuclease, ATP-dependent unwinding and DNA-dependent ATPase activities. Strand cleavage occurs 5' to 3' during the unwinding of duplex DNA at CHI sequences, which locally stimulate recombination. [EX5C_ECOLI] Exhibits a wide variety of catalytic activities including ATP-dependent exonuclease, ATP-stimulated endonuclease, ATP-dependent helicase and DNA-dependent ATPase activities. 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 molecular mechanism of superfamily 1Balpha helicases remains unclear. We present here the crystal structure of the RecD2 helicase from Deinococcus radiodurans at 2.2-A resolution. The structure reveals the folds of the 1B and 2B domains of RecD that were poorly ordered in the structure of the Escherichia coli RecBCD enzyme complex reported previously. The 2B domain adopts an SH3 fold which, although common in eukaryotes, is extremely rare in bacterial systems. In addition, the D. radiodurans RecD2 structure has aided us in deciphering lower resolution (3.6 A) electron density maps for the E. coli RecBCD enzyme in complex with a long DNA substrate that interacts with the RecD subunit. Taken together, these structures indicated an important role for the 1B domain of RecD, a beta-hairpin that extends from the surface of the 1A domain and interacts with the DNA substrate. On the basis of these structural data, we designed a mutant RecD2 helicase that lacks this pin. The 'pin-less' mutant protein is a fully active ssDNA-dependent ATPase but totally lacks helicase activity. DNA binding to RecD: role of the 1B domain in SF1B helicase activity.,Saikrishnan K, Griffiths SP, Cook N, Court R, Wigley DB EMBO J. 2008 Aug 20;27(16):2222-9. Epub 2008 Jul 31. PMID:18668125 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Exonuclease

Proteopedia Page Contributors and Editors (what is this?)

OCA