3Q3V
Crystal structure of Phosphoglycerate Kinase from Campylobacter jejuni.
3Q3V の概要
| エントリーDOI | 10.2210/pdb3q3v/pdb |
| 分子名称 | Phosphoglycerate kinase, POTASSIUM ION, FORMIC ACID, ... (6 entities in total) |
| 機能のキーワード | structural genomics, center for structural genomics of infectious diseases, csgid, pgk, converts 3-phospho-d-glycerate to 3-phospho-d-glyceroyl phosphate during the glycolysis pathway, transferase |
| 由来する生物種 | Campylobacter jejuni subsp. jejuni NCTC 11168 |
| 細胞内の位置 | Cytoplasm : Q9PMQ5 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 89614.08 |
| 構造登録者 | Filippova, E.V.,Wawrzak, Z.,Onopriyenko, O.,Edwards, A.,Savchenko, A.,Anderson, W.F.,Center for Structural Genomics of Infectious Diseases (CSGID) (登録日: 2010-12-22, 公開日: 2011-01-12, 最終更新日: 2024-11-06) |
| 主引用文献 | Zheng, H.,Filippova, E.V.,Tkaczuk, K.L.,Dworzynski, P.,Chruszcz, M.,Porebski, P.J.,Wawrzak, Z.,Onopriyenko, O.,Kudritska, M.,Grimshaw, S.,Savchenko, A.,Anderson, W.F.,Minor, W. Crystal structures of putative phosphoglycerate kinases from B. anthracis and C. jejuni. J.Struct.Funct.Genom., 13:15-26, 2012 Cited by PubMed Abstract: Phosphoglycerate kinase (PGK) is indispensable during glycolysis for anaerobic glucose degradation and energy generation. Here we present comprehensive structure analysis of two putative PGKs from Bacillus anthracis str. Sterne and Campylobacter jejuni in the context of their structural homologs. They are the first PGKs from pathogenic bacteria reported in the Protein Data Bank. The crystal structure of PGK from Bacillus anthracis str. Sterne (BaPGK) has been determined at 1.68 Å while the structure of PGK from Campylobacter jejuni (CjPGK) has been determined at 2.14 Å resolution. The proteins' monomers are composed of two domains, each containing a Rossmann fold, hinged together by a helix which can be used to adjust the relative position between two domains. It is also shown that apo-forms of both BaPGK and CjPGK adopt open conformations as compared to the substrate and ATP bound forms of PGK from other species. PubMed: 22403005DOI: 10.1007/s10969-012-9131-9 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.145 Å) |
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