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3GMT

Crystal structure of adenylate kinase from burkholderia pseudomallei

3GMT の概要
エントリーDOI10.2210/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
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: 20331978
DOI: 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)
構造検証レポート
Validation report summary of 3gmt
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-12-31に公開中

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