5K4P
Catalytic Domain of MCR-1 phosphoethanolamine transferase
5K4P の概要
| エントリーDOI | 10.2210/pdb5k4p/pdb |
| 分子名称 | Probable phosphatidylethanolamine transferase Mcr-1, ZINC ION, sorbitol, ... (4 entities in total) |
| 機能のキーワード | phosphoethanolamine transferase, alpha/beta/alpha fold, alkaline phosphatase superfamily, transferase |
| 由来する生物種 | Escherichia coli BL21(DE3) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 39345.18 |
| 構造登録者 | Stojanoski, V.,Palzkill, T.,Prasad, B.V.V.,Sankaran, B. (登録日: 2016-05-21, 公開日: 2016-08-31, 最終更新日: 2024-10-09) |
| 主引用文献 | Stojanoski, V.,Sankaran, B.,Prasad, B.V.,Poirel, L.,Nordmann, P.,Palzkill, T. Structure of the catalytic domain of the colistin resistance enzyme MCR-1. Bmc Biol., 14:81-81, 2016 Cited by PubMed Abstract: Due to the paucity of novel antibiotics, colistin has become a last resort antibiotic for treating multidrug resistant bacteria. Colistin acts by binding the lipid A component of lipopolysaccharides and subsequently disrupting the bacterial membrane. The recently identified plasmid-encoded MCR-1 enzyme is the first transmissible colistin resistance determinant and is a cause for concern for the spread of this resistance trait. MCR-1 is a phosphoethanolamine transferase that catalyzes the addition of phosphoethanolamine to lipid A to decrease colistin affinity. PubMed: 27655155DOI: 10.1186/s12915-016-0303-0 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.318 Å) |
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