3zyt: Difference between revisions
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==Structure Determination of EstA from Arthrobacter nitroguajacolicus Rue61a== | |||
<StructureSection load='3zyt' size='340' side='right'caption='[[3zyt]], [[Resolution|resolution]] 2.45Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3zyt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Paenarthrobacter_nitroguajacolicus Paenarthrobacter nitroguajacolicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZYT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZYT FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.45Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EMC:ETHYL+MERCURY+ION'>EMC</scene></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=3zyt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zyt OCA], [https://pdbe.org/3zyt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zyt RCSB], [https://www.ebi.ac.uk/pdbsum/3zyt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zyt ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/K4DIE4_PAENT K4DIE4_PAENT] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
In this article we analyze the reasons for catalytic promiscuity of a type VIII esterase with beta-lactamase fold and the ability to cleave beta-lactams. We compared the structure of this enzyme to those of an esterase of the same type without any lactamase ability, an esterase with moderate lactamase ability, and a class C beta-lactamase with similar fold. Our results show that for these enzymes, the difference in the substrate specificity is sterically driven. | |||
Crystal structure analysis of EstA from Arthrobacter sp. Rue61a--an insight into catalytic promiscuity.,Wagner UG, DiMaio F, Kolkenbrock S, Fetzner S FEBS Lett. 2014 Apr 2;588(7):1154-60. doi: 10.1016/j.febslet.2014.02.045. Epub, 2014 Mar 5. PMID:24613918<ref>PMID:24613918</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3zyt" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Paenarthrobacter nitroguajacolicus]] | ||
[[Category: Fetzner S]] | |||
[[Category: Wagner UG]] | |||