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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 [ | <table><tr><td colspan='2'>[[3s4x]] is a 1 chain structure with sequence from [https://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 [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='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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ampC ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ampC ([https://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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Beta-lactamase Beta-lactamase], with EC number [https://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'>[ | <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> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[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;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 22: | Line 22: | ||
==See Also== | ==See Also== | ||
*[[Beta-lactamase|Beta-lactamase]] | *[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 28: | Line 28: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Beta-lactamase]] | [[Category: Beta-lactamase]] | ||
[[Category: Large Structures]] | |||
[[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 13:38, 22 June 2022
Crystal structure of the Asn152Gly mutant of P99 beta-lactamaseCrystal structure of the Asn152Gly mutant of P99 beta-lactamase
Structural highlights
Function[AMPC_ENTCL] This protein is a serine beta-lactamase with a substrate specificity for cephalosporins. Publication Abstract from PubMedP99 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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