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<StructureSection load='7kcw' size='340' side='right'caption='[[7kcw]], [[Resolution|resolution]] 1.73&Aring;' scene=''>
<StructureSection load='7kcw' size='340' side='right'caption='[[7kcw]], [[Resolution|resolution]] 1.73&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7kcw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_COL Staphylococcus aureus subsp. aureus COL]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7KCW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7KCW FirstGlance]. <br>
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7KCW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7KCW 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]] 1.73&#8491;</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.73&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NFF:(2R,4S)-2-[(1R)-1-{[(2-ETHOXYNAPHTHALEN-1-YL)CARBONYL]AMINO}-2-OXOETHYL]-5,5-DIMETHYL-1,3-THIAZOLIDINE-4-CARBOXYLIC+ACID'>NFF</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NFF:(2R,4S)-2-[(1R)-1-{[(2-ETHOXYNAPHTHALEN-1-YL)CARBONYL]AMINO}-2-OXOETHYL]-5,5-DIMETHYL-1,3-THIAZOLIDINE-4-CARBOXYLIC+ACID'>NFF</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=7kcw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7kcw OCA], [https://pdbe.org/7kcw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7kcw RCSB], [https://www.ebi.ac.uk/pdbsum/7kcw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7kcw ProSAT]</span></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=7kcw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7kcw OCA], [https://pdbe.org/7kcw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7kcw RCSB], [https://www.ebi.ac.uk/pdbsum/7kcw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7kcw ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0H2WY27_STAAC A0A0H2WY27_STAAC]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
BACKGROUND: PBP4, a low-molecular-weight PBP in Staphylococcus aureus, is not considered to be a classical mediator of beta-lactam resistance. Previous studies carried out by our group with laboratory strains of S. aureus demonstrated the ability of PBP4 to produce beta-lactam resistance through mutations associated with the pbp4 promoter and/or gene. Recent studies of beta-lactam-resistant clinical isolates of S. aureus have reported similar mutations associated with pbp4. OBJECTIVES: To determine if pbp4-associated mutations reported among clinical strains of S. aureus mediate beta-lactam resistance. METHODS: The pbp4 promoters and genes bearing mutations from clinical isolates were cloned into a heterologous host. Reporter, growth and Bocillin assays were performed to assess their role in beta-lactam resistance. X-ray crystallography was used to obtain acyl-enzyme intermediate structures of the WT and mutant PBP4 with nafcillin and cefoxitin. RESULTS: Of the five strains that contained pbp4 promoter mutations, three strains exhibited enhanced expression of PBP4. The R200L mutation in pbp4 resulted in increased survival in the presence of the beta-lactams nafcillin and cefoxitin. Further, introduction of either a promoter or a gene mutation into the genome of a WT host increased the ability of the strains to resist the action of beta-lactams. The four high-resolution X-ray structures presented demonstrate the binding pose of the beta-lactams tested and provide hints for further drug development. CONCLUSIONS: Mutations associated with the pbp4 promoter and pbp4 gene altered protein activity and mediated beta-lactam resistance among the clinically isolated strains that were studied.
PBP4-mediated beta-lactam resistance among clinical strains of Staphylococcus aureus.,Satishkumar N, Alexander JAN, Poon R, Buggeln E, Argudin MA, Strynadka NCJ, Chatterjee SS J Antimicrob Chemother. 2021 Jun 21. pii: 6307153. doi: 10.1093/jac/dkab201. PMID:34151961<ref>PMID:34151961</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7kcw" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Penicillin-binding protein 3D structures|Penicillin-binding protein 3D structures]]
*[[Penicillin-binding protein 3D structures|Penicillin-binding protein 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Staphylococcus aureus subsp. aureus COL]]
[[Category: Alexander JA]]
[[Category: Alexander JA]]
[[Category: Strynadka NC]]
[[Category: Strynadka NC]]
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