8g02
From Proteopedia
YES Complex - E. coli MraY, Protein E PhiX174, E. coli SlyD
Structural highlights
FunctionMRAY_ECOLI Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I.[HAMAP-Rule:MF_00038][1] [2] Publication Abstract from PubMedThe historically important phage PhiX174 kills its host bacteria by encoding a 91-residue protein antibiotic called protein E. Using single-particle electron cryo-microscopy, we demonstrate that protein E bridges two bacterial proteins to form the transmembrane YES complex [MraY, protein E, sensitivity to lysis D (SlyD)]. Protein E inhibits peptidoglycan biosynthesis by obstructing the MraY active site leading to loss of lipid I production. We experimentally validate this result for two different viral species, providing a clear model for bacterial lysis and unifying previous experimental data. Additionally, we characterize the Escherichia coli MraY structure-revealing features of this essential enzyme-and the structure of the chaperone SlyD bound to a protein. Our structures provide insights into the mechanism of phage-mediated lysis and for structure-based design of phage therapeutics. The mechanism of the phage-encoded protein antibiotic from PhiX174.,Orta AK, Riera N, Li YE, Tanaka S, Yun HG, Klaic L, Clemons WM Jr Science. 2023 Jul 14;381(6654):eadg9091. doi: 10.1126/science.adg9091. Epub 2023 , Jul 14. PMID:37440661[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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