2XF4
Crystal structure of Salmonella enterica serovar typhimurium YcbL
2XF4 の概要
| エントリーDOI | 10.2210/pdb2xf4/pdb |
| 分子名称 | HYDROXYACYLGLUTATHIONE HYDROLASE, ZINC ION, TETRAETHYLENE GLYCOL, ... (4 entities in total) |
| 機能のキーワード | hydrolase |
| 由来する生物種 | SALMONELLA ENTERICA |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 23378.77 |
| 構造登録者 | Stamp, A.,Owen, P.,El Omari, K.,Nichols, C.,Lockyer, M.,Lamb, H.,Charles, I.,Hawkins, A.R.,Stammers, D.K. (登録日: 2010-05-20, 公開日: 2010-07-28, 最終更新日: 2024-05-08) |
| 主引用文献 | Stamp, A.,Owen, P.,El Omari, K.,Nichols, C.,Lockyer, M.,Lamb, H.,Charles, I.,Hawkins, A.R.,Stammers, D.K. Structural and Functional Characterization of Salmonella Enterica Serovar Typhimurium Ycbl: An Unusual Type II Glyoxalase Protein Sci., 19:1897-, 2010 Cited by PubMed Abstract: YcbL has been annotated as either a metallo-β-lactamase or glyoxalase II (GLX2), both members of the zinc metallohydrolase superfamily, that contains many enzymes with a diverse range of activities. Here, we report crystallographic and biochemical data for Salmonella enterica serovar Typhimurium YcbL that establishes it as GLX2, which differs in certain structural and functional properties compared with previously known examples. These features include the insertion of an α-helix after residue 87 in YcbL and truncation of the C-terminal domain, which leads to the loss of some recognition determinants for the glutathione substrate. Despite these changes, YcbL has robust GLX2 activity. A further difference is that the YcbL structure contains only a single bound metal ion rather than the dual site normally observed for GLX2s. Activity assays in the presence of various metal ions indicate an increase in activity above basal levels in the presence of manganous and ferrous ions. Thus, YcbL represents a novel member of the GLX2 family. PubMed: 20669241DOI: 10.1002/PRO.475 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.3 Å) |
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