1QOJ

Crystal Structure of E.coli UvrB C-terminal domain, and a model for UvrB-UvrC interaction.

Summary for 1QOJ

• Entry DOI: 10.2210/pdb1qoj/pdb
• Related: 1E52
• Descriptor: UVRB (1 entity in total)
• Functional Keywords: dna excision repair, nucleotide excision repair, uvrb protein, uvrb-c interaction
• Biological source: ESCHERICHIA COLI
• Total number of polymer chains: 2
• Total formula weight: 15371.87

Authors

Sohi, M.,Alexandrovich, A.,Moolenaar, G.,Visse, R.,Goosen, N.,Vernede, X.,Fontecilla-Camps, J.,Champness, J.,Sanderson, M.R. (deposition date: 1999-11-10, release date: 2000-11-10, Last modification date: 2024-11-20)

Primary citation

Sohi, M.,Alexandrovich, A.,Moolenaar, G.,Visse, R.,Goosen, N.,Vernede, X.,Fontecilla-Camps, J.,Champness, J.,Sanderson, M.R.
Crystal Structure of E.Coli Uvrb C-Terminal Domain, and a Model for Uvrb-Uvrc Interaction
FEBS Lett., 465:161-, 2000

PubMed Abstract: A 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.

PubMed: 10631326
DOI: 10.1016/S0014-5793(99)01690-7

Experimental method

X-RAY DIFFRACTION (3 Å)