1qoj | pdb_00001qoj
From Proteopedia
CRYSTAL STRUCTURE OF E.COLI UVRB C-TERMINAL DOMAIN, AND A MODEL FOR UVRB-UVRC INTERACTION.
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Structural highlights
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 PubMedA crystal structure of the C-terminal domain of Escherichia coli UvrB (UvrB') has been solved to 3.0 A resolution. The domain adopts a helix-loop-helix fold which is stabilised by the packing of hydrophobic side-chains between helices. From the UvrB' fold, a model for a domain of UvrC (UvrC') that has high sequence homology with UvrB' has been made. In the crystal, a dimerisation of UvrB domains is seen involving specific hydrophobic and salt bridge interactions between residues in and close to the loop region of the domain. It is proposed that a homologous mode of interaction may occur between UvrB and UvrC. This interaction is likely to be flexible, potentially spanning > 50 A. Crystal structure of Escherichia coli UvrB C-terminal domain, and a model for UvrB-uvrC interaction.,Sohi M, Alexandrovich A, Moolenaar G, Visse R, Goosen N, Vernede X, Fontecilla-Camps JC, Champness J, Sanderson MR FEBS Lett. 2000 Jan 14;465(2-3):161-4. PMID:10631326[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferencesContents | ||||||||||||||||||||
This page was last modified 14:22, 29 September 2014.