1ola
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(New page: 200px<br /><applet load="1ola" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ola, resolution 2.1Å" /> '''THE STRUCTURAL BASIS ...)
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Revision as of 20:52, 20 November 2007
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THE STRUCTURAL BASIS OF MULTISPECIFICITY IN THE OLIGOPEPTIDE-BINDING PROTEIN OPPA
Overview
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.
About this Structure
1OLA is a Single protein structure of sequence from Salmonella typhimurium with IUM as ligand. Full crystallographic information is available from OCA.
Reference
The structural basis of sequence-independent peptide binding by OppA protein., Tame JR, Murshudov GN, Dodson EJ, Neil TK, Dodson GG, Higgins CF, Wilkinson AJ, Science. 1994 Jun 10;264(5165):1578-81. PMID:8202710
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