3zyt
From Proteopedia
(Difference between revisions)
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<StructureSection load='3zyt' size='340' side='right' caption='[[3zyt]], [[Resolution|resolution]] 2.45Å' scene=''> | <StructureSection load='3zyt' size='340' side='right' caption='[[3zyt]], [[Resolution|resolution]] 2.45Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3zyt]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[3zyt]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Artnt Artnt]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ZYT FirstGlance]. <br> |
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EMC:ETHYL+MERCURY+ION'>EMC</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EMC:ETHYL+MERCURY+ION'>EMC</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3zyt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zyt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3zyt RCSB], [http://www.ebi.ac.uk/pdbsum/3zyt PDBsum]</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=3zyt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zyt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3zyt RCSB], [http://www.ebi.ac.uk/pdbsum/3zyt PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
| + | <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. | ||
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| + | 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> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Artnt]] |
[[Category: Fetzner, S.]] | [[Category: Fetzner, S.]] | ||
[[Category: Wagner, U G.]] | [[Category: Wagner, U G.]] | ||
Revision as of 08:45, 22 October 2014
Structure Determination of EstA from Arthrobacter nitroguajacolicus Rue61a
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