View source for 6k8x


==Crystal structure of a class C beta lactamase==
<StructureSection load='6k8x' size='340' side='right'caption='[[6k8x]], [[Resolution|resolution]] 1.59&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6k8x]] 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=6K8X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6K8X 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]] 1.59&#8491;</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=6k8x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6k8x OCA], [https://pdbe.org/6k8x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6k8x RCSB], [https://www.ebi.ac.uk/pdbsum/6k8x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6k8x ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9XB24_KLEPN Q9XB24_KLEPN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
ACC-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<ref>PMID:31451494</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6k8x" style="background-color:#fffaf0;"></div>

==See Also==
*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Klebsiella pneumoniae]]
[[Category: Large Structures]]
[[Category: An YJ]]
[[Category: Bae DW]]
[[Category: Cha SS]]
[[Category: Jung YE]]
[[Category: Na JH]]