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 ConservationCheck, 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 AlsoReferences | ||||||||||||||||||||
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