3DUV
Crystal structure of 3-deoxy-manno-octulosonate cytidylyltransferase from Haemophilus influenzae complexed with the substrate 3-deoxy-manno-octulosonate in the-configuration
3DUV の概要
| エントリーDOI | 10.2210/pdb3duv/pdb |
| 分子名称 | 3-deoxy-manno-octulosonate cytidylyltransferase, 3-deoxy-alpha-D-manno-oct-2-ulopyranosonic acid, O-ACETALDEHYDYL-HEXAETHYLENE GLYCOL, ... (4 entities in total) |
| 機能のキーワード | cmp-kdo synthetase, 3-deoxy-manno-octulosonate cytidylyltransferase, 3-deoxy-manno-octulosonate, kdsb, cytoplasm, lipopolysaccharide biosynthesis, nucleotidyltransferase, transferase |
| 由来する生物種 | Haemophilus influenzae |
| 細胞内の位置 | Cytoplasm (Potential): P44490 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 59986.77 |
| 構造登録者 | |
| 主引用文献 | Yoon, H.J.,Ku, M.J.,Mikami, B.,Suh, S.W. Structure of 3-deoxy-manno-octulosonate cytidylyltransferase from Haemophilus influenzae complexed with the substrate 3-deoxy-manno-octulosonate in the beta-configuration. Acta Crystallogr.,Sect.D, 64:1292-1294, 2008 Cited by PubMed Abstract: The enzyme 3-deoxy-manno-octulosonate cytidylyltransferase (CMP-KDO synthetase; CKS) catalyzes the activation of 3-deoxy-D-manno-octulosonate (or 2-keto-3-deoxy-manno-octonic acid; KDO) by forming CMP-KDO. CKS is unique to Gram-negative bacteria and is an attractive target for the development of antibacterial agents. The crystal structure of CKS from Haemophilus influenzae in complex with the substrate KDO has been determined at 2.30 A resolution by combining single-wavelength anomalous diffraction and molecular-replacement methods. The two monomers in the asymmetric unit differ in the conformation of their C-terminal alpha-helix (Ala230-Asn254). The KDO bound to the active site exists as the beta-pyranose form in the (5)C(2) chair conformation. The structure of CKS from H. influenzae in complex with KDO will be useful in structure-based inhibitor design. PubMed: 19018107DOI: 10.1107/S0907444908036342 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.3 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード






