2WOL
Clavulanic acid biosynthesis oligopeptide binding protein 2
2WOL の概要
| エントリーDOI | 10.2210/pdb2wol/pdb |
| 関連するPDBエントリー | 2WOK 2WOP |
| 分子名称 | CLAVULANIC ACID BIOSYNTHESIS OLIGOPEPTIDE BINDING PROTEIN 2, GLYCEROL (3 entities in total) |
| 機能のキーワード | peptide binding protein, solute-binding protein, clavulanic acid biosynthesis, oligopeptide binding protein |
| 由来する生物種 | STREPTOMYCES CLAVULIGERUS |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 62341.84 |
| 構造登録者 | MacKenzie, A.K.,Valegard, K.,Iqbal, A.,Caines, M.E.C.,Kershaw, N.J.,Jensen, S.E.,Schofield, C.J.,Andersson, I. (登録日: 2009-07-27, 公開日: 2009-12-08, 最終更新日: 2024-05-08) |
| 主引用文献 | Mackenzie, A.K.,Valegard, K.,Iqbal, A.,Caines, M.E.C.,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-, 2010 Cited by 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: 19941870DOI: 10.1016/J.JMB.2009.11.045 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.45 Å) |
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