View source for 8ehu


==Crystal structure of the environmental CRH-1 class A carbapenemase at 1.1 Angstrom resolution==
<StructureSection load='8ehu' size='340' side='right'caption='[[8ehu]], [[Resolution|resolution]] 1.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8ehu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Chromobacterium_haemolyticum Chromobacterium haemolyticum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8EHU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8EHU 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]] 1.1&#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=8ehu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ehu OCA], [https://pdbe.org/8ehu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ehu RCSB], [https://www.ebi.ac.uk/pdbsum/8ehu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ehu ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A1W0D7S2_9NEIS A0A1W0D7S2_9NEIS] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
KPC-2 is one of the most relevant serine-carbapenemases among the carbapenem-resistant Enterobacterales. We previously isolated from the environmental species Chromobacterium haemolyticum a class A CRH-1 beta-lactamase displaying 69% amino acid sequence identity with KPC-2. The objective of this study was to analyze the kinetic behavior and crystallographic structure of this beta-lactamase. Our results showed that CRH-1 can hydrolyze penicillins, cephalosporins (except ceftazidime), and carbapenems with similar efficacy compared to KPC-2. Inhibition kinetics showed that CRH-1 is not well inhibited by clavulanic acid, in contrast to efficient inhibition by avibactam (AVI). The high-resolution crystal of the apoenzyme showed that CRH-1 has a similar folding compared to other class A beta-lactamases. The CRH-1/AVI complex showed that AVI adopts a chair conformation, stabilized by hydrogen bonds to Ser70, Ser237, Asn132, and Thr235. Our findings highlight the biochemical and structural similarities of CRH-1 and KPC-2 and the potential clinical impact of this carbapenemase in the event of recruitment by pathogenic bacterial species.

Biochemical and Structural Characterization of CRH-1, a Carbapenemase from Chromobacterium haemolyticum Related to KPC beta-Lactamases.,Brunetti F, Ghiglione B, Gudeta DD, Gutkind G, Guardabassi L, Klinke S, Power P Antimicrob Agents Chemother. 2023 Jul 18;67(7):e0006123. doi: , 10.1128/aac.00061-23. Epub 2023 Jun 5. PMID:37272821<ref>PMID:37272821</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8ehu" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Chromobacterium haemolyticum]]
[[Category: Large Structures]]
[[Category: Brunetti F]]
[[Category: Ghiglione B]]
[[Category: Guardabassi L]]
[[Category: Gutkind G]]
[[Category: Klinke S]]
[[Category: Power P]]