5XJ6
Crystal structure of PlsY (YgiH), an integral membrane glycerol 3-phosphate acyltransferase - the glycerol 3-phosphate form
5XJ6 の概要
エントリーDOI | 10.2210/pdb5xj6/pdb |
関連するPDBエントリー | 5XJ5 5XJ7 5XJ8 5XJ9 |
分子名称 | Glycerol-3-phosphate acyltransferase, SN-GLYCEROL-3-PHOSPHATE, (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate, ... (5 entities in total) |
機能のキーワード | glycerol 3-phosphate acyltransferase, glycerylphosphate acyltransferase, gpat, in meso, lipid cubic phase, lipidic cubic phase, lipid metabolism, monoacylglycerol, phospholipid biosynthesis, plsy, substrate, ygih, transferase |
由来する生物種 | Aquifex aeolicus |
細胞内の位置 | Cell inner membrane ; Multi-pass membrane protein : O66905 |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 23585.21 |
構造登録者 | |
主引用文献 | Li, Z.,Tang, Y.,Wu, Y.,Zhao, S.,Bao, J.,Luo, Y.,Li, D. Structural insights into the committed step of bacterial phospholipid biosynthesis. Nat Commun, 8:1691-1691, 2017 Cited by PubMed Abstract: The membrane-integral glycerol 3-phosphate (G3P) acyltransferase PlsY catalyses the committed and essential step in bacterial phospholipid biosynthesis by acylation of G3P, forming lysophosphatidic acid. It contains no known acyltransferase motifs, lacks eukaryotic homologs, and uses the unusual acyl-phosphate as acyl donor, as opposed to acyl-CoA or acyl-carrier protein for other acyltransferases. Previous studies have identified several PlsY inhibitors as potential antimicrobials. Here we determine the crystal structure of PlsY at 1.48 Å resolution, revealing a seven-transmembrane helix fold. Four additional substrate- and product-bound structures uncover the atomic details of its relatively inflexible active site. Structure and mutagenesis suggest a different acylation mechanism of 'substrate-assisted catalysis' that, unlike other acyltransferases, does not require a proteinaceous catalytic base to complete. The structure data and a high-throughput enzymatic assay developed in this work should prove useful for virtual and experimental screening of inhibitors against this vital bacterial enzyme. PubMed: 29167463DOI: 10.1038/s41467-017-01821-9 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.37 Å) |
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