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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]] 1.95&Aring;' scene=''>
<StructureSection load='3s4x' size='340' side='right'caption='[[3s4x]], [[Resolution|resolution]] 1.95&Aring;' 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]] 1.95&#8491;</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.
 
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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3s4x" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Beta-lactamase|Beta-lactamase]]
*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
== References ==
<references/>
__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]]

Latest revision as of 15:46, 14 March 2024

Crystal structure of the Asn152Gly mutant of P99 beta-lactamaseCrystal structure of the Asn152Gly mutant of P99 beta-lactamase

Structural highlights

3s4x is a 1 chain structure with sequence from Enterobacter cloacae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.95Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

AMPC_ENTCL This protein is a serine beta-lactamase with a substrate specificity for cephalosporins.

See Also

3s4x, resolution 1.95Å

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