6fcs
From Proteopedia
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- | '''Unreleased structure''' | ||
- | The | + | ==The X-ray Structure of Lytic Transglycosylase Slt inactive mutant E503Q from Pseudomonas aeruginosa in complex with NAG-NAMpentapeptide-NAG-NAMpentapeptide== |
+ | <StructureSection load='6fcs' size='340' side='right'caption='[[6fcs]], [[Resolution|resolution]] 2.90Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[6fcs]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FCS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6FCS FirstGlance]. <br> | ||
+ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9Å</td></tr> | ||
+ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=66N:L-ALANINAMIDE'>66N</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=AMU:BETA-N-ACETYLMURAMIC+ACID'>AMU</scene>, <scene name='pdbligand=AMV:METHYL+2-(ACETYLAMINO)-3-O-[(1R)-1-CARBOXYETHYL]-2-DEOXY-BETA-D-GLUCOPYRANOSIDE'>AMV</scene>, <scene name='pdbligand=API:2,6-DIAMINOPIMELIC+ACID'>API</scene>, <scene name='pdbligand=DAL:D-ALANINE'>DAL</scene>, <scene name='pdbligand=DGL:D-GLUTAMIC+ACID'>DGL</scene>, <scene name='pdbligand=MAG:BETA-METHYL-N-ACETYL-D-GLUCOSAMINE'>MAG</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NM6:(2R)-2-[(2R,3S,4R,5R,6R)-5-ACETAMIDO-2-(HYDROXYMETHYL)-3,6-BIS(OXIDANYL)OXAN-4-YL]OXYPROPANAMIDE'>NM6</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=6fcs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fcs OCA], [https://pdbe.org/6fcs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6fcs RCSB], [https://www.ebi.ac.uk/pdbsum/6fcs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6fcs ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/Q9HZI6_PSEAE Q9HZI6_PSEAE] | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | beta-Lactam antibiotics inhibit cell-wall transpeptidases, preventing the peptidoglycan, the major constituent of the bacterial cell wall, from cross-linking. This causes accumulation of long non-cross-linked strands of peptidoglycan, which leads to bacterial death. Pseudomonas aeruginosa, a nefarious bacterial pathogen, attempts to repair this aberrantly formed peptidoglycan by the function of the lytic transglycosylase Slt. We document in this report that Slt turns over the peptidoglycan by both exolytic and endolytic reactions, which cause glycosidic bond scission from a terminus or in the middle of the peptidoglycan, respectively. These reactions were characterized with complex synthetic peptidoglycan fragments that ranged in size from tetrasaccharides to octasaccharides. The X-ray structure of the wild-type apo Slt revealed it to be a doughnut-shaped protein. In a series of six additional X-ray crystal structures, we provide insights with authentic substrates into how Slt is enabled for catalysis for both the endolytic and exolytic reactions. The substrate for the exolytic reaction binds Slt in a canonical arrangement and reveals how both the glycan chain and the peptide stems are recognized by the Slt. We document that the apo enzyme does not have a fully formed active site for the endolytic reaction. However, binding of the peptidoglycan at the existing subsites within the catalytic domain causes a conformational change in the protein that assembles the surface for binding of a more expansive peptidoglycan between the catalytic domain and an adjacent domain. The complexes of Slt with synthetic peptidoglycan substrates provide an unprecedented snapshot of the endolytic reaction. | ||
- | + | Exolytic and endolytic turnover of peptidoglycan by lytic transglycosylase Slt of Pseudomonas aeruginosa.,Lee M, Batuecas MT, Tomoshige S, Dominguez-Gil T, Mahasenan KV, Dik DA, Hesek D, Millan C, Uson I, Lastochkin E, Hermoso JA, Mobashery S Proc Natl Acad Sci U S A. 2018 Apr 9. pii: 1801298115. doi:, 10.1073/pnas.1801298115. PMID:29632171<ref>PMID:29632171</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | [[Category: | + | </div> |
- | [[Category: | + | <div class="pdbe-citations 6fcs" style="background-color:#fffaf0;"></div> |
- | [[Category: Dominguez-Gil | + | == References == |
- | [[Category: | + | <references/> |
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Pseudomonas aeruginosa]] | ||
+ | [[Category: Batuecas MT]] | ||
+ | [[Category: Dominguez-Gil T]] | ||
+ | [[Category: Hermoso JA]] |
Current revision
The X-ray Structure of Lytic Transglycosylase Slt inactive mutant E503Q from Pseudomonas aeruginosa in complex with NAG-NAMpentapeptide-NAG-NAMpentapeptide
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