8g02: Difference between revisions
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==YES Complex - E. coli MraY, Protein E PhiX174, E. coli SlyD== | |||
<StructureSection load='8g02' size='340' side='right'caption='[[8g02]], [[Resolution|resolution]] 3.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8g02]] 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_phiX174 Escherichia phage phiX174]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8G02 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8G02 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]] 3.5Å</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=8g02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8g02 OCA], [https://pdbe.org/8g02 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8g02 RCSB], [https://www.ebi.ac.uk/pdbsum/8g02 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8g02 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> | ||
[[Category: Clemons | <div class="pdbe-citations 8g02" style="background-color:#fffaf0;"></div> | ||
[[Category: Li | == References == | ||
[[Category: Orta | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli K-12]] | |||
[[Category: Escherichia phage phiX174]] | |||
[[Category: Large Structures]] | |||
[[Category: Clemons WM]] | |||
[[Category: Li YE]] | |||
[[Category: Orta AK]] | |||
