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| | ==Crystal structure of the Asn152Gly mutant of P99 beta-lactamase== | | ==Crystal structure of the Asn152Gly mutant of P99 beta-lactamase== |
| - | <StructureSection load='3s4x' size='340' side='right' caption='[[3s4x]], [[Resolution|resolution]] 1.95Å' scene=''> | + | <StructureSection load='3s4x' size='340' side='right'caption='[[3s4x]], [[Resolution|resolution]] 1.95Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3s4x]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"aerobacter_cloacae"_(jordan_1890)_bergey_et_al._1923 "aerobacter cloacae" (jordan 1890) bergey et al. 1923]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3S4X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3S4X FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3s4x]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterobacter_cloacae Enterobacter cloacae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3S4X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3S4X FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ampC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=550 "Aerobacter cloacae" (Jordan 1890) Bergey et al. 1923])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3s4x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s4x OCA], [https://pdbe.org/3s4x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3s4x RCSB], [https://www.ebi.ac.uk/pdbsum/3s4x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3s4x 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=3s4x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s4x OCA], [http://pdbe.org/3s4x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3s4x RCSB], [http://www.ebi.ac.uk/pdbsum/3s4x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3s4x ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/AMPC_ENTCL AMPC_ENTCL]] This protein is a serine beta-lactamase with a substrate specificity for cephalosporins. | + | [https://www.uniprot.org/uniprot/AMPC_ENTCL AMPC_ENTCL] This protein is a serine beta-lactamase with a substrate specificity for cephalosporins. |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | P99 cephalosporinase is a class C beta-lactamase that is responsible in part for the widespread bacterial resistance to beta-lactam antibiotics. Mutations of the conserved active-site residue Asn152 of the enzyme have been shown to alter beta-lactam substrate specificity in vivo. Mutation of Asn152 to a glycine is notable in that it exhibits in vivo substrate-selectivity switching. In order to better understand the structural basis for this observed switch, the X-ray crystal structure of the apo Asn152Gly mutant of P99 was determined to 1.95 A resolution. Unexpectedly, the artificial C-terminal His(6) tag of a symmetrically-related molecule was observed bound in the active site. The His(6) tag makes several interactions with key active-site residues, as well as with several sulfate ions. Additionally, the overall C-terminus occupies the space left vacant upon the mutation of Asn152 to glycine.
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| - | Structural analysis of the Asn152Gly mutant of P99 cephalosporinase.,Ruble JF, Lefurgy ST, Cornish VW, Powers RA Acta Crystallogr D Biol Crystallogr. 2012 Sep;68(Pt 9):1189-93. doi:, 10.1107/S0907444912024080. Epub 2012 Aug 18. PMID:22948919<ref>PMID:22948919</ref>
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| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
| + | |
| - | <div class="pdbe-citations 3s4x" style="background-color:#fffaf0;"></div>
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Beta-lactamase|Beta-lactamase]] | + | *[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]] |
| - | == References ==
| + | |
| - | <references/>
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Beta-lactamase]] | + | [[Category: Enterobacter cloacae]] |
| - | [[Category: Powers, R A]] | + | [[Category: Large Structures]] |
| - | [[Category: Ruble, J F]] | + | [[Category: Powers RA]] |
| - | [[Category: Cephalosporinase]] | + | [[Category: Ruble JF]] |
| - | [[Category: Hydrolase]]
| + | |
