3s4x
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | [[ | + | ==Crystal structure of the Asn152Gly mutant of P99 beta-lactamase== |
| + | <StructureSection load='3s4x' size='340' side='right' caption='[[3s4x]], [[Resolution|resolution]] 1.95Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3s4x]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/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> | ||
| + | <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 Enterobacter cloacae])</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'>[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://www.rcsb.org/pdb/explore.do?structureId=3s4x RCSB], [http://www.ebi.ac.uk/pdbsum/3s4x PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| - | + | ==See Also== | |
| - | + | *[[Beta-lactamase|Beta-lactamase]] | |
| - | == | + | == References == |
| - | [[ | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Beta-lactamase]] | [[Category: Beta-lactamase]] | ||
[[Category: Enterobacter cloacae]] | [[Category: Enterobacter cloacae]] | ||
| - | [[Category: Powers, R A | + | [[Category: Powers, R A]] |
| - | [[Category: Ruble, J F | + | [[Category: Ruble, J F]] |
[[Category: Cephalosporinase]] | [[Category: Cephalosporinase]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
Revision as of 11:44, 9 December 2014
Crystal structure of the Asn152Gly mutant of P99 beta-lactamase
| |||||||||||
