PDBsum entry 2wok

Peptide binding protein/peptide

PDB id: 2wok

Contents

Protein chain

553 a.a. *

Ligands

ARG-PRO-PRO-GLY-PHE

ARG

GOL ×2

Waters ×380

* Residue conservation analysis

PDB id:

2wok

Name:

Peptide binding protein/peptide

Title:

Clavulanic acid biosynthesis oligopeptide binding protein 2 complexed with bradykinin

Structure:

Clavulanic acid biosynthesis oligopeptide binding protein 2. Chain: a. Synonym: orf15. Engineered: yes. Kininogen-1. Chain: b. Synonym: bradykinin,alpha-2-thiol proteinase inhibitor,fitzgerald factor,high molecular weight kininogen,hmwk,williams-fitzgerald-

Source:

Streptomyces clavuligerus. Organism_taxid: 1901. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Synthetic: yes. Homo sapiens. Human. Organism_taxid: 9606

Resolution:

1.70Å R-factor: 0.187 R-free: 0.223

Authors:

A.K.Mackenzie,K.Valegard,A.Iqbal,M.E.C.Caines,N.J.Kershaw,S.E.Jensen, C.J.Schofield,I.Andersson

Key ref:

A.K.Mackenzie et al. (2010). Crystal structures of an oligopeptide-binding protein from the biosynthetic pathway of the beta-lactamase inhibitor clavulanic acid. J Mol Biol, 396, 332-344. PubMed id: 19941870

Date:

26-Jul-09 Release date: 08-Dec-09

Protein chain

Q8KRB4  (Q8KRB4_STRCL) -  ABC-type dipeptide transport system, solute-binding protein from Streptomyces clavuligerus

Seq: 562 a.a.

Struc: 553 a.a.

J Mol Biol 396:332-344 (2010)

PubMed id: 19941870

Crystal structures of an oligopeptide-binding protein from the biosynthetic pathway of the beta-lactamase inhibitor clavulanic acid.

A.K.Mackenzie, K.Valegård, A.Iqbal, M.E.Caines, N.J.Kershaw, S.E.Jensen, C.J.Schofield, I.Andersson.

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.