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-Structure paper
タイトル | The mechanism of the phage-encoded protein antibiotic from ΦX174. |
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ジャーナル・号・ページ | Science, Vol. 381, Issue 6654, Page eadg9091, Year 2023 |
掲載日 | 2023年7月14日 |
![]() | Anna K Orta / Nadia Riera / Yancheng E Li / Shiho Tanaka / Hyun Gi Yun / Lada Klaic / William M Clemons / ![]() |
PubMed 要旨 | The historically important phage ΦX174 kills its host bacteria by encoding a 91-residue protein antibiotic called protein E. Using single-particle electron cryo-microscopy, we demonstrate that ...The historically important phage ΦX174 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 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. |
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手法 | EM (単粒子) |
解像度 | 3.4 - 3.5 Å |
構造データ | EMDB-29641, PDB-8g01: EMDB-29642: YES Complex - E. coli MraY, Protein E ID21, E. coli SlyD |
由来 |
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![]() | TRANSFERASE/ISOMERASE / inhibitor / antibiotic / chaperone / membrane / bacteriophage / TRANSFERASE-ISOMERASE complex |