2JG1
STRUCTURE OF Staphylococcus aureus D-TAGATOSE-6-PHOSPHATE KINASE with cofactor and substrate
2JG1 の概要
エントリーDOI | 10.2210/pdb2jg1/pdb |
関連するPDBエントリー | 2JGV |
分子名称 | TAGATOSE-6-PHOSPHATE KINASE, MAGNESIUM ION, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (5 entities in total) |
機能のキーワード | d-tagatose-6-phosphate kinase, phosphoryl transfer, conformational changes, kinase, transferase, lactose metabolism |
由来する生物種 | STAPHYLOCOCCUS AUREUS |
タンパク質・核酸の鎖数 | 4 |
化学式量合計 | 147707.18 |
構造登録者 | Miallau, L.,Hunter, W.N.,McSweeney, S.M.,Leonard, G.A. (登録日: 2007-02-07, 公開日: 2007-04-24, 最終更新日: 2024-11-13) |
主引用文献 | Miallau, L.,Hunter, W.N.,Mcsweeney, S.M.,Leonard, G.A. Structures of Staphylococcus Aureus D-Tagatose-6-Phosphate Kinase Implicate Domain Motions in Specificity and Mechanism. J.Biol.Chem., 282:19948-, 2007 Cited by PubMed Abstract: High resolution structures of Staphylococcus aureus d-tagatose-6-phosphate kinase (LacC) in two crystal forms are herein reported. The structures define LacC in apoform, in binary complexes with ADP or the co-factor analogue AMP-PNP, and in a ternary complex with AMP-PNP and D-tagatose-6-phosphate. The tertiary structure of the LacC monomer, which is closely related to other members of the pfkB subfamily of carbohydrate kinases, is composed of a large alpha/beta core domain and a smaller, largely beta "lid." Four extended polypeptide segments connect these two domains. Dimerization of LacC occurs via interactions between lid domains, which come together to form a beta-clasp structure. Residues from both subunits contribute to substrate binding. LacC adopts a closed structure required for phosphoryl transfer only when both substrate and co-factor are bound. A reaction mechanism similar to that used by other phosphoryl transferases is proposed, although unusually, when both substrate and co-factor are bound to the enzyme two Mg(2+) ions are observed in the active site. A new motif of amino acid sequence conservation common to the pfkB subfamily of carbohydrate kinases is identified. PubMed: 17459874DOI: 10.1074/JBC.M701480200 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2 Å) |
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