3zyt: Difference between revisions

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== Structural highlights ==

<table><tr><td colspan='2'>[[3zyt]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Arthrobacter_nitroguajacolicus Arthrobacter 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ZYT FirstGlance]. <br>

<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><br>

</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>

== 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>

== References ==

__TOC__

</StructureSection>

[[Category: ~~Arthrobacter nitroguajacolicus~~]]

[[Category: Artnt]]

[[Category: Fetzner, S.]]

[[Category: Wagner, U G.]]

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@@ Line 2: / Line 2: @@
 <StructureSection load='3zyt' size='340' side='right' caption='[[3zyt]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3zyt]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arthrobacter_nitroguajacolicus Arthrobacter 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ZYT FirstGlance]. <br>
+<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><br>
+</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.
+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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+== References ==
+<references/>
 __TOC__
 </StructureSection>
-[[Category: Arthrobacter nitroguajacolicus]]
+[[Category: Artnt]]
 [[Category: Fetzner, S.]]
 [[Category: Wagner, U G.]]