3GMT
Crystal structure of adenylate kinase from burkholderia pseudomallei
3GMT の概要
| エントリーDOI | 10.2210/pdb3gmt/pdb |
| 分子名称 | Adenylate kinase, SULFATE ION (3 entities in total) |
| 機能のキーワード | ssgcid, adenylate kinase, burkholderia pseudomallei, atp-binding, kinase, nucleotide biosynthesis, nucleotide-binding, transferase, structural genomics, seattle structural genomics center for infectious disease |
| 由来する生物種 | Burkholderia pseudomallei 1710b |
| 細胞内の位置 | Cytoplasm (By similarity): Q3JVB1 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 51927.30 |
| 構造登録者 | Abendroth, J.,Staker, B.L.,Robinson, H.,Buchko, G.W.,Hewitt, S.N.,Napuli, A.J.,Van Voorhis, W.,Stacy, R.,Myler, P.J.,Stewart, L.,Seattle Structural Genomics Center for Infectious Disease (SSGCID) (登録日: 2009-03-15, 公開日: 2009-06-02, 最終更新日: 2024-11-06) |
| 主引用文献 | Buchko, G.W.,Robinson, H.,Abendroth, J.,Staker, B.L.,Myler, P.J. Structural characterization of Burkholderia pseudomallei adenylate kinase (Adk): profound asymmetry in the crystal structure of the 'open' state. Biochem.Biophys.Res.Commun., 394:1012-1017, 2010 Cited by PubMed Abstract: In all organisms adenylate kinases (Adks) play a vital role in cellular energy metabolism and nucleic acid synthesis. Due to differences in catalytic properties between the Adks found in prokaryotes and in the cytoplasm of eukaryotes, there is interest in targeting this enzyme for new drug therapies against infectious bacterial agents. Here we report the 2.1A resolution crystal structure for the 220-residue Adk from Burkholderia pseudomallei (BpAdk), the etiological agent responsible for the infectious disease melioidosis. The general structure of apo BpAdk is similar to other Adk structures, composed of a CORE subdomain with peripheral ATP-binding (ATP(bd)) and LID subdomains. The two molecules in the asymmetric unit have significantly different conformations, with a backbone RMSD of 1.46 A. These two BpAdk conformations may represent 'open' Adk sub-states along the preferential pathway to the 'closed' substrate-bound state. PubMed: 20331978DOI: 10.1016/j.bbrc.2010.03.112 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.1 Å) |
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