1OLA

THE STRUCTURAL BASIS OF MULTISPECIFICITY IN THE OLIGOPEPTIDE-BINDING PROTEIN OPPA

Summary for 1OLA

• Entry DOI: 10.2210/pdb1ola/pdb
• Descriptor: OLIGO-PEPTIDE BINDING PROTEIN, PEPTIDE VAL-LYS-PRO-GLY, URANYL (VI) ION, ... (4 entities in total)
• Functional Keywords: binding protein
• Biological source: Salmonella typhimurium
• Cellular location: Periplasm: P06202
• Total number of polymer chains: 2
• Total formula weight: 59819.53

Authors

Tame, J.,Wilkinson, A.J. (deposition date: 1994-04-26, release date: 1994-07-31, Last modification date: 2024-10-30)

Primary citation

Tame, J.R.,Murshudov, G.N.,Dodson, E.J.,Neil, T.K.,Dodson, G.G.,Higgins, C.F.,Wilkinson, A.J.
The structural basis of sequence-independent peptide binding by OppA protein.
Science, 264:1578-1581, 1994

PubMed Abstract: 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.

PubMed: 8202710

Experimental method

X-RAY DIFFRACTION (2.1 Å)