6ka5: Difference between revisions
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<StructureSection load='6ka5' size='340' side='right'caption='[[6ka5]], [[Resolution|resolution]] 1.59Å' scene=''> | <StructureSection load='6ka5' size='340' side='right'caption='[[6ka5]], [[Resolution|resolution]] 1.59Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6ka5]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KA5 OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[6ka5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Klebsiella_pneumoniae Klebsiella pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KA5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6KA5 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1S7:(2R)-2-{(1S)-1-METHOXY-2-OXO-1-[(THIOPHEN-2-YLACETYL)AMINO]ETHYL}-5-METHYLIDENE-5,6-DIHYDRO-2H-1,3-THIAZINE-4-CARBOXYLIC+ACID'>1S7</scene | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.59Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1S7:(2R)-2-{(1S)-1-METHOXY-2-OXO-1-[(THIOPHEN-2-YLACETYL)AMINO]ETHYL}-5-METHYLIDENE-5,6-DIHYDRO-2H-1,3-THIAZINE-4-CARBOXYLIC+ACID'>1S7</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6ka5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ka5 OCA], [https://pdbe.org/6ka5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ka5 RCSB], [https://www.ebi.ac.uk/pdbsum/6ka5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ka5 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q9XB24_KLEPN Q9XB24_KLEPN] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 17: | Line 19: | ||
</div> | </div> | ||
<div class="pdbe-citations 6ka5" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 6ka5" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Klebsiella pneumoniae]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: An | [[Category: An YJ]] | ||
[[Category: Bae | [[Category: Bae DW]] | ||
[[Category: Cha | [[Category: Cha SS]] | ||
[[Category: Jung | [[Category: Jung YE]] | ||
[[Category: Na | [[Category: Na JH]] | ||
Latest revision as of 17:36, 29 November 2023
Crystal structure of a class C beta-lactamase in complex with cefoxitinCrystal structure of a class C beta-lactamase in complex with cefoxitin
Structural highlights
FunctionPublication Abstract from PubMedACC-1 is a plasmid-encoded class C beta-lactamase identified in clinical isolates of Klebsiella pneumoniae, Proteus mirabilis, Salmonella enterica, and Escherichia coli ACC-1-producing bacteria are susceptible to cefoxitin whereas they are resistant to oxyimino cephalosporins. Here, we depict crystal structures of apo ACC-1, adenylylated ACC-1, and acylated ACC-1 complexed with cefotaxime and cefoxitin. ACC-1 has noteworthy structural alterations in the R2-loop, the Omega- loop, and the Phe119-loop along the active-site rim. The adenylate covalently bonded to the nucleophilic serine reveals a tetrahedral phosphorus mimicking the deacylation transition state. Cefotaxime in ACC-1 has a proper conformation for the substrate-assisted catalysis in that its C4 carboxylate and N5 nitrogen are adequately located to facilitate the deacylation reaction. In contrast, cefoxitin in ACC-1 has a distinct conformation in which those functional groups cannot contribute to catalysis. Furthermore, the orientation of the deacylating water relative to the acyl carbonyl group in ACC-1 is unfavorable for nucleophilic attack. Structural insights into catalytic relevances of substrates' poses in ACC-1.,Bae DW, Jung YE, An YJ, Na JH, Cha SS Antimicrob Agents Chemother. 2019 Aug 26. pii: AAC.01411-19. doi:, 10.1128/AAC.01411-19. PMID:31451494[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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