4MKS
Crystal structure of enolase from Lactobacillus gasseri
4MKS の概要
| エントリーDOI | 10.2210/pdb4mks/pdb |
| 関連するPDBエントリー | 1w6t 4a3r 4ewj |
| 分子名称 | Enolase 2, CHLORIDE ION, MAGNESIUM ION, ... (4 entities in total) |
| 機能のキーワード | enolase, lyase |
| 由来する生物種 | Lactobacillus gasseri |
| 細胞内の位置 | Cytoplasm (By similarity): Q042F4 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 96086.99 |
| 構造登録者 | Raghunathan, K.,Harris, P.T.,Spurbeck, R.R.,Arvidson, C.G.,Arvidson, D.N. (登録日: 2013-09-05, 公開日: 2014-05-21, 最終更新日: 2023-09-20) |
| 主引用文献 | Raghunathan, K.,Harris, P.T.,Spurbeck, R.R.,Arvidson, C.G.,Arvidson, D.N. Crystal structure of an efficacious gonococcal adherence inhibitor: An enolase from Lactobacillus gasseri. Febs Lett., 588:2212-2216, 2014 Cited by PubMed Abstract: Enolases are highly conserved metalloenzymes ubiquitous to cellular metabolism. While these enzymes share a large degree of sequence and structural similarity, they have been shown to possess a wide range of moonlighting functions. Recent studies showed that an enolase from Lactobacillus gasseri impedes the ability of Neisseria gonorrhoeae to adhere to epithelial cells. We present the crystal structure of this enolase, the first from Lactobacillus, with one of its Mg(2+) cofactors. Determined using molecular replacement to 2.08Å, the structure has a flexible and surface exposed catalytic loop containing lysines, and may play a role in the inhibitory function. PubMed: 24859038DOI: 10.1016/j.febslet.2014.05.020 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.079 Å) |
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