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Science 10 June 1994:
Vol. 264. no. 5165, pp. 1578 - 1581
DOI: 10.1126/science.8202710
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Articles

Science, Vol 264, Issue 5165, 1578-1581
Copyright © 1994 by American Association for the Advancement of Science

articles

The structural basis of sequence-independent peptide binding by OppA protein

Tame JR, GN Murshudov, EJ Dodson, TK Neil, GG Dodson, CF Higgins, and AJ Wilkinson

Department of Chemistry, University of York, UK.

Specific protein-ligand interactions are critical for cellular function, and most proteins select their partners with sharp discrimination. However, the oligopeptide-binding protein of Salmonella typhimurium (OppA) binds peptides of two to five amino acid residues without regard to sequence. The crystal structure of OppA reveals a three-domain organization, unlike other periplasmic binding proteins. In OppA-peptide complexes, the ligands are completely enclosed in the protein interior, a mode of binding that normally imposes tight specificity. The protein fulfills the hydrogen bonding and electrostatic potential of the ligand main chain and accommodates the peptide side chains in voluminous hydrated cavities.


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