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4rm5

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Revision as of 18:47, 24 December 2014

Structural and mechanistic insights into NDM-1 catalyzed hydrolysis of cephalosporins

Structural highlights

4rm5 is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Activity:	Beta-lactamase, with EC number 3.5.2.6
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[BLAN1_KLEPN] Confers resistance to many beta-lactam antibiotics, including some carbapenems. Does not confer resistance to the polymixin colistin or the fluoroquinolone ciprofloxacin.

Publication Abstract from PubMed

Cephalosporins constitute a large class of beta-lactam antibiotics clinically used as antimicrobial drugs. New Dehli metallo-beta-lactamase (NDM-1) poses a global threat to human health as it confers on bacterial pathogen resistance to almost all beta-lactams, including penicillins, cephalosporins, and carbapenems. Here we report the first crystal structures of NDM-1 in complex with cefuroxime and cephalexin, as well as NMR spectra monitoring cefuroxime and cefixime hydrolysis catalyzed by NDM-1. Surprisingly, cephalosporoate intermediates were captured in both crystal structures determined at 1.3 and 2.0 A. These results provide detailed information concerning the mechanism and pathways of cephalosporin hydrolysis. We also present the crystal structure and enzyme assays of a D124N mutant, which reveals that D124 most likely plays a more structural than catalytic role.

Structural and Mechanistic Insights into NDM-1 Catalyzed Hydrolysis of Cephalosporins.,Feng H, Ding J, Zhu D, Liu X, Xu X, Zhang Y, Zang S, Wang DC, Liu W J Am Chem Soc. 2014 Oct 22;136(42):14694-7. doi: 10.1021/ja508388e. Epub 2014 Oct, 7. PMID:25268575^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Feng H, Ding J, Zhu D, Liu X, Xu X, Zhang Y, Zang S, Wang DC, Liu W. Structural and Mechanistic Insights into NDM-1 Catalyzed Hydrolysis of Cephalosporins. J Am Chem Soc. 2014 Oct 22;136(42):14694-7. doi: 10.1021/ja508388e. Epub 2014 Oct, 7. PMID:25268575 doi:http://dx.doi.org/10.1021/ja508388e

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4rm5"

@@ Line 7: / Line 7: @@
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4rm5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rm5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4rm5 RCSB], [http://www.ebi.ac.uk/pdbsum/4rm5 PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/BLAN1_KLEPN BLAN1_KLEPN]] Confers resistance to many beta-lactam antibiotics, including some carbapenems. Does not confer resistance to the polymixin colistin or the fluoroquinolone ciprofloxacin.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

4rm5

From Proteopedia

Revision as of 18:47, 24 December 2014

Structural and mechanistic insights into NDM-1 catalyzed hydrolysis of cephalosporins

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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