3a15
From Proteopedia
(Difference between revisions)
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<StructureSection load='3a15' size='340' side='right'caption='[[3a15]], [[Resolution|resolution]] 1.79Å' scene=''> | <StructureSection load='3a15' size='340' side='right'caption='[[3a15]], [[Resolution|resolution]] 1.79Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3a15]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[3a15]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodococcus_erythropolis Rhodococcus erythropolis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A15 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3A15 FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.79Å</td></tr> |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr> | |
| - | <tr id=' | + | |
| - | + | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3a15 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a15 OCA], [https://pdbe.org/3a15 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3a15 RCSB], [https://www.ebi.ac.uk/pdbsum/3a15 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3a15 ProSAT]</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=3a15 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a15 OCA], [https://pdbe.org/3a15 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3a15 RCSB], [https://www.ebi.ac.uk/pdbsum/3a15 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3a15 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/OXD_RHOER OXD_RHOER] Catalyzes the dehydration of aldoximes to their corresponding nitrile (PubMed:16233624, PubMed:19740758). Is active toward various arylalkyl- and alkyl-aldoximes, and to a lesser extent toward aryl-aldoximes (PubMed:16233624).<ref>PMID:16233624</ref> <ref>PMID:19740758</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3a15 ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3a15 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Aldoxime dehydratase (Oxd) catalyzes the dehydration of aldoximes (R-CH=N-OH) to their corresponding nitrile (R-C triple bond N). Oxd is a heme-containing enzyme that catalyzes the dehydration reaction as its physiological function. We have determined the first two structures of Oxd: the substrate-free OxdRE at 1.8 A resolution and the n-butyraldoxime- and propionaldoxime-bound OxdREs at 1.8 and 1.6 A resolutions, respectively. Unlike other heme enzymes, the organic substrate is directly bound to the heme iron in OxdRE. We determined the structure of the Michaelis complex of OxdRE by using the unique substrate binding and activity regulation properties of Oxd. The Michaelis complex was prepared by x-ray cryoradiolytic reduction of the ferric dead-end complex in which Oxd contains a Fe(3+) heme form. The crystal structures reveal the mechanism of substrate recognition and the catalysis of OxdRE. | ||
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| - | X-ray crystal structure of michaelis complex of aldoxime dehydratase.,Sawai H, Sugimoto H, Kato Y, Asano Y, Shiro Y, Aono S J Biol Chem. 2009 Nov 13;284(46):32089-96. Epub 2009 Sep 8. PMID:19740758<ref>PMID:19740758</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 3a15" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Mycobacterium erythropolis gray and thornton 1928]] | ||
| - | [[Category: Aliphatic aldoxime dehydratase]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Aono | + | [[Category: Rhodococcus erythropolis]] |
| - | [[Category: Asano | + | [[Category: Aono S]] |
| - | [[Category: Kato | + | [[Category: Asano Y]] |
| - | [[Category: Sawai | + | [[Category: Kato Y]] |
| - | [[Category: Shiro | + | [[Category: Sawai H]] |
| - | [[Category: Sugimoto | + | [[Category: Shiro Y]] |
| - | + | [[Category: Sugimoto H]] | |
| - | + | ||
| - | + | ||
Current revision
Crystal Structure of Substrate-Free Form of Aldoxime Dehydratase (OxdRE)
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