8g01
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==YES Complex - E. coli MraY, Protein E ID21, E. coli SlyD== | |
| + | <StructureSection load='8g01' size='340' side='right'caption='[[8g01]], [[Resolution|resolution]] 3.40Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8g01]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12] and [https://en.wikipedia.org/wiki/Escherichia_phage_ID21 Escherichia phage ID21]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8G01 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8G01 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.4Å</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8g01 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8g01 OCA], [https://pdbe.org/8g01 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8g01 RCSB], [https://www.ebi.ac.uk/pdbsum/8g01 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8g01 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/MRAY_ECOLI MRAY_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]<ref>PMID:1846850</ref> <ref>PMID:215212</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The 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<ref>PMID:37440661</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 8g01" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Escherichia coli K-12]] | ||
| + | [[Category: Escherichia phage ID21]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Clemons WM]] | ||
| + | [[Category: Orta AK]] | ||
| + | [[Category: Riera N]] | ||
Revision as of 12:38, 26 July 2023
YES Complex - E. coli MraY, Protein E ID21, E. coli SlyD
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