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| | <StructureSection load='4d2o' size='340' side='right'caption='[[4d2o]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='4d2o' size='340' side='right'caption='[[4d2o]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4d2o]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacterium_freundii"_braak_1928 "bacterium freundii" braak 1928]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3znw 3znw]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D2O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4D2O FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4d2o]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Citrobacter_freundii Citrobacter freundii]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3znw 3znw]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D2O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4D2O FirstGlance]. <br> |
| - | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-lactamase Beta-lactamase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.6 3.5.2.6] </span></td></tr> | + | </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=4d2o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d2o OCA], [https://pdbe.org/4d2o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4d2o RCSB], [https://www.ebi.ac.uk/pdbsum/4d2o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4d2o ProSAT]</span></td></tr> |
| - | <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=4d2o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d2o OCA], [http://pdbe.org/4d2o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4d2o RCSB], [http://www.ebi.ac.uk/pdbsum/4d2o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4d2o ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [[https://www.uniprot.org/uniprot/A2RP81_CITFR A2RP81_CITFR]] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Beta-lactamase|Beta-lactamase]] | + | *[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacterium freundii braak 1928]] | + | [[Category: Citrobacter freundii]] |
| - | [[Category: Beta-lactamase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Charlier, P]] | + | [[Category: Charlier P]] |
| - | [[Category: Galleni, M]] | + | [[Category: Galleni M]] |
| - | [[Category: Gutkind, G]] | + | [[Category: Gutkind G]] |
| - | [[Category: Herman, R]] | + | [[Category: Herman R]] |
| - | [[Category: Kerff, F]] | + | [[Category: Kerff F]] |
| - | [[Category: Power, P]] | + | [[Category: Power P]] |
| - | [[Category: Ruggiero, M]] | + | [[Category: Ruggiero M]] |
| - | [[Category: Sauvage, E]] | + | [[Category: Sauvage E]] |
| - | [[Category: Cefotaximase]]
| + | |
| - | [[Category: Esbl]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Oxyimino-cephalosporinase]]
| + | |
| Structural highlights
Function
[A2RP81_CITFR]
Publication Abstract from PubMed
PER-2 belongs to a small (7 members to date) group of extended-spectrum beta-lactamases. It has 88% amino acid identity with PER-1 and both display high catalytic efficiencies towards most beta-lactams. In this study, we determined the X-ray structure of PER-2 at 2.20 A, and evaluated the possible role of several residues in the structure and activity towards beta-lactams and mechanism-based inhibitors. PER-2 is defined by the presence of a singular trans bond between residues 166-167 that generates an inverted Omega loop, and an expanded fold of this domain that results in a wide active site cavity that allows for an efficient hydrolysis of antibiotics like the oxyimino-cephalosporins, and a series of exclusive interactions between residues not frequently involved in the stabilization of the active site in other class A beta-lactamases. PER beta-lactamases could be included within a cluster of evolutionary related enzymes harboring conserved residues Asp136 and Asn179. Other signature residues that define these enzymes seem to be Gln69, Arg220, Thr237, and probably Arg/Lys240A, with structurally important roles in the stabilization of the active site and proper orientation of catalytic water molecules, among others. We propose, supported by simulated models of PER-2 in combination with different beta-lactams, the presence of a hydrogen-bond network connecting Ser70-Gln69-Water-Thr237-Arg220 that might be important for the proper activity and inhibition of the enzyme. Therefore, we could expect that mutations occurring in these positions will have impact in the overall hydrolytic behavior.
Crystal Structure of the Extended-Spectrum beta-Lactamase PER-2 and Insights into the Role of Specific Residues in the Interaction with beta-Lactams and beta-Lactamase Inhibitors.,Ruggiero M, Kerff F, Herman R, Sapunaric F, Galleni M, Gutkind G, Charlier P, Sauvage E, Power P Antimicrob Agents Chemother. 2014 Jul 28. pii: AAC.00089-14. PMID:25070104[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ruggiero M, Kerff F, Herman R, Sapunaric F, Galleni M, Gutkind G, Charlier P, Sauvage E, Power P. Crystal Structure of the Extended-Spectrum beta-Lactamase PER-2 and Insights into the Role of Specific Residues in the Interaction with beta-Lactams and beta-Lactamase Inhibitors. Antimicrob Agents Chemother. 2014 Jul 28. pii: AAC.00089-14. PMID:25070104 doi:http://dx.doi.org/10.1128/AAC.00089-14
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