9c3f
From Proteopedia
(Difference between revisions)
m (Protected "9c3f" [edit=sysop:move=sysop]) |
|||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Cryo-EM structure of E. coli AmpG== | |
| + | <StructureSection load='9c3f' size='340' side='right'caption='[[9c3f]], [[Resolution|resolution]] 3.78Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[9c3f]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9C3F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9C3F 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]] 3.78Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene>, <scene name='pdbligand=PEE:1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOETHANOLAMINE'>PEE</scene></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=9c3f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9c3f OCA], [https://pdbe.org/9c3f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9c3f RCSB], [https://www.ebi.ac.uk/pdbsum/9c3f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9c3f ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/C562_ECOLX C562_ECOLX] Electron-transport protein of unknown function.[https://www.uniprot.org/uniprot/AMPG_ECOLI AMPG_ECOLI] Permease involved in cell wall peptidoglycan recycling (PubMed:12426329, PubMed:8878601). Transports, from the periplasm into the cytoplasm, the disaccharide N-acetylglucosaminyl-beta-1,4-anhydro-N-acetylmuramic acid (GlcNAc-anhMurNAc) and GlcNAc-anhMurNAc-peptides (PubMed:12426329). Transport is dependent on the proton motive force (PubMed:12426329). AmpG is also involved in beta-lactamase induction (PubMed:7773404).<ref>PMID:12426329</ref> <ref>PMID:7773404</ref> <ref>PMID:8878601</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Bacteria invest significant resources into the continuous creation and tailoring of their essential protective peptidoglycan (PG) cell wall. Several soluble PG biosynthesis products in the periplasm are transported to the cytosol for recycling, leading to enhanced bacterial fitness. GlcNAc-1,6-anhydroMurNAc and peptide variants are transported by the essential major facilitator superfamily importer AmpG in Gram-negative pathogens including Escherichia coli, Klebsiella pneumoniae, Acinetobacter baumannii, and Pseudomonas aeruginosa. Accumulation of GlcNAc-1,6-anhydroMurNAc-pentapeptides also results from beta-lactam antibiotic induced cell wall damage. In some species, these products upregulate the beta-lactamase AmpC, which hydrolyzes beta-lactams to allow for bacterial survival and drug-resistant infections. Here, we have used cryo-electron microscopy and chemical synthesis of substrates in an integrated structural, biochemical, and cellular analysis of AmpG. We show how AmpG accommodates the large GlcNAc-1,6-anhydroMurNAc peptides, including a unique hydrophobic vestibule to the substrate binding cavity, and characterize residues involved in binding that inform the mechanism of proton-mediated transport. | ||
| - | + | Cryo-EM characterization of the anydromuropeptide permease AmpG central to bacterial fitness and beta-lactam antibiotic resistance.,Sverak HE, Yaeger LN, Worrall LJ, Vacariu CM, Glenwright AJ, Vuckovic M, Al Azawi ZD, Lamers RP, Marko VA, Skorupski C, Soni AS, Tanner ME, Burrows LL, Strynadka NC Nat Commun. 2024 Nov 16;15(1):9936. doi: 10.1038/s41467-024-54219-9. PMID:39548104<ref>PMID:39548104</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 9c3f" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Escherichia coli]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Strynadka NCJ]] | ||
| + | [[Category: Sverak H]] | ||
| + | [[Category: Worrall LJ]] | ||
Revision as of 06:30, 18 December 2024
Cryo-EM structure of E. coli AmpG
| |||||||||||
