2rec

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RECA HEXAMER MODEL, ELECTRON MICROSCOPYRECA HEXAMER MODEL, ELECTRON MICROSCOPY

Structural highlights

2rec is a 6 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Electron Microscopy
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RECA_ECOLI Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage.[HAMAP-Rule:MF_00268]

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 RecA protein forms a hexameric ring that is similar to the core of the F1-ATPase. Several lines of evidence suggest that this hexamer may be a structural homologue of ring helicases.

The RecA hexamer is a structural homologue of ring helicases.,Yu X, Egelman EH Nat Struct Biol. 1997 Feb;4(2):101-4. PMID:9033586[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Yu X, Egelman EH. The RecA hexamer is a structural homologue of ring helicases. Nat Struct Biol. 1997 Feb;4(2):101-4. PMID:9033586
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