5XJ6

Crystal structure of PlsY (YgiH), an integral membrane glycerol 3-phosphate acyltransferase - the glycerol 3-phosphate form

Summary for 5XJ6

• Entry DOI: 10.2210/pdb5xj6/pdb
• Related: 5XJ5 5XJ7 5XJ8 5XJ9
• Descriptor: Glycerol-3-phosphate acyltransferase, SN-GLYCEROL-3-PHOSPHATE, (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate, ... (5 entities in total)
• Functional Keywords: glycerol 3-phosphate acyltransferase, glycerylphosphate acyltransferase, gpat, in meso, lipid cubic phase, lipidic cubic phase, lipid metabolism, monoacylglycerol, phospholipid biosynthesis, plsy, substrate, ygih, transferase
• Biological source: Aquifex aeolicus
• Cellular location: Cell inner membrane ; Multi-pass membrane protein : O66905
• Total number of polymer chains: 1
• Total formula weight: 23585.21

Authors

Li, Z.,Tang, Y.,Li, D. (deposition date: 2017-04-30, release date: 2017-12-06, Last modification date: 2024-03-27)

Primary citation

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

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: 29167463
DOI: 10.1038/s41467-017-01821-9

Experimental method

X-RAY DIFFRACTION (2.37 Å)