2WOK

Clavulanic acid biosynthesis oligopeptide binding protein 2 complexed with bradykinin

Summary for 2WOK

• Entry DOI: 10.2210/pdb2wok/pdb
• Related: 2WOL 2WOP
• Descriptor: CLAVULANIC ACID BIOSYNTHESIS OLIGOPEPTIDE BINDING PROTEIN 2, Kininogen-1, GLYCEROL, ... (4 entities in total)
• Functional Keywords: peptide binding protein-peptide complex, solute-binding protein, clavulanic acid biosynthesis, oligopeptide binding protein, oligopeptide, bradykinin, peptide binding protein/peptide
• Biological source: Streptomyces clavuligerus; More
• Total number of polymer chains: 2
• Total formula weight: 63311.97

Authors

Mackenzie, A.K.,Valegard, K.,Iqbal, A.,Caines, M.E.C.,Kershaw, N.J.,Jensen, S.E.,Schofield, C.J.,Andersson, I. (deposition date: 2009-07-26, release date: 2009-12-08, Last modification date: 2023-12-20)

Primary citation

Mackenzie, A.K.,Valegard, K.,Iqbal, A.,Caines, M.E.,Kershaw, N.J.,Jensen, S.E.,Schofield, C.J.,Andersson, I.
Crystal structures of an oligopeptide-binding protein from the biosynthetic pathway of the beta-lactamase inhibitor clavulanic acid.
J. Mol. Biol., 396:332-344, 2010

PubMed Abstract: Clavulanic acid (CA) is a clinically important beta-lactamase inhibitor that is produced by fermentation of Streptomyces clavuligerus. The CA biosynthesis pathway starts from arginine and glyceraldehyde-3-phosphate and proceeds via (3S,5S)-clavaminic acid, which is converted to (3R,5R)-clavaldehyde, the immediate precursor of (3R,5R)-CA. Open reading frames 7 (orf7) and 15 (orf15) of the CA biosynthesis cluster encode oligopeptide-binding proteins (OppA1 and OppA2), which are essential for CA biosynthesis. OppA1/2 are proposed to be involved in the binding and/or transport of peptides across the S. clavuligerus cell membrane. Peptide binding assays reveal that recombinant OppA1 and OppA2 bind di-/tripeptides containing arginine and certain nonapeptides including bradykinin. Crystal structures of OppA2 in its apo form and in complex with arginine or bradykinin were solved to 1.45, 1.7, and 1.7 A resolution, respectively. The overall fold of OppA2 consists of two lobes with a deep cavity in the center, as observed for other oligopeptide-binding proteins. The large cavity creates a peptide/arginine binding cleft. The crystal structures of OppA2 in complex with arginine or bradykinin reveal that the C-terminal arginine of bradykinin binds similarly to arginine. The results are discussed in terms of the possible roles of OppA1/2 in CA biosynthesis.

PubMed: 19941870
DOI: 10.1016/j.jmb.2009.11.045

Experimental method

X-RAY DIFFRACTION (1.7 Å)