1V1B
2-KETO-3-DEOXYGLUCONATE KINASE FROM THERMUS THERMOPHILUS WITH BOUND ATP
1V1B の概要
エントリーDOI | 10.2210/pdb1v1b/pdb |
関連するPDBエントリー | 1J5V 1V19 1V1A |
分子名称 | 2-KETO-3-DEOXYGLUCONATE KINASE, ADENOSINE-5'-TRIPHOSPHATE (3 entities in total) |
機能のキーワード | 2-keto-3-deoxygluconate kinase, atp, thermus thermophilus, structural genomics, transferase, riken structural genomics/proteomics initiative, rsgi |
由来する生物種 | THERMUS THERMOPHILUS |
タンパク質・核酸の鎖数 | 4 |
化学式量合計 | 135909.46 |
構造登録者 | |
主引用文献 | Ohshima, N.,Inagaki, E.,Yasuike, K.,Takio, K.,Tahirov, T.H. Structure of Thermus thermophilus 2-Keto-3-deoxygluconate kinase: evidence for recognition of an open chain substrate. J. Mol. Biol., 340:477-489, 2004 Cited by PubMed Abstract: 2-Keto-3-deoxygluconate kinase (KDGK) catalyzes the phosphorylation of 2-keto-3-deoxygluconate (KDG) to 2-keto-3-deoxy-6-phosphogluconate (KDGP). The genome sequence of Thermus thermophilus HB8 contains an open reading frame that has a 30% identity to Escherichia coli KDGK. The KDGK activity of T.thermophilus protein (TtKDGK) has been confirmed, and its crystal structure has been determined by the molecular replacement method and refined with two crystal forms to 2.3 angstroms and 3.2 angstroms, respectively. The enzyme is a hexamer organized as a trimer of dimers. Each subunit is composed of two domains, a larger alpha/beta domain and a smaller beta-sheet domain, similar to that of ribokinase and adenosine kinase, members of the PfkB family of carbohydrate kinases. Furthermore, the TtKDGK structure with its KDG and ATP analogue was determined and refined at 2.1 angstroms. The bound KDG was observed predominantly as an open chain structure. The positioning of ligands and the conservation of important catalytic residues suggest that the reaction mechanism is likely to be similar to that of other members of the PfkB family, including ribokinase. In particular, the Asp251 is postulated to have a role in transferring the gamma-phosphate of ATP to the 5'-hydroxyl group of KDG. PubMed: 15210349DOI: 10.1016/j.jmb.2004.04.074 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.6 Å) |
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