1lzl
From Proteopedia
(Difference between revisions)
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<StructureSection load='1lzl' size='340' side='right'caption='[[1lzl]], [[Resolution|resolution]] 1.30Å' scene=''> | <StructureSection load='1lzl' size='340' side='right'caption='[[1lzl]], [[Resolution|resolution]] 1.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[1lzl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1lzl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodococcus_sp. Rhodococcus sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LZL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LZL 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]] 1.3Å</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=1lzl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lzl OCA], [https://pdbe.org/1lzl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lzl RCSB], [https://www.ebi.ac.uk/pdbsum/1lzl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lzl 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=1lzl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lzl OCA], [https://pdbe.org/1lzl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lzl RCSB], [https://www.ebi.ac.uk/pdbsum/1lzl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lzl ProSAT]</span></td></tr> | ||
</table> | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/O06441_RHOSO O06441_RHOSO] | ||
== 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=1lzl 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=1lzl ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | The crystal structures of an acetyl esterase, HerE, and its complex with an inhibitor dimethylarsinic acid have been determined at 1.30- and 1.45-A resolution, respectively. Although the natural substrate for the enzyme is unknown, HerE hydrolyzes the acetyl groups from heroin to yield morphine and from phenyl acetate to yield phenol. Recently, the activity of the enzyme toward heroin has been exploited to develop a heroin biosensor, which affords higher sensitivity than other currently available detection methods. The crystal structure reveals a single domain with the canonical alpha/beta hydrolase fold with an acyl binding pocket that snugly accommodates the acetyl substituent of the substrate and three backbone amides that form a tripartite oxyanion hole. In addition, a covalent adduct was observed between the active site serine and dimethylarsinic acid, which inhibits the enzyme. This crystal structure provides the first example of an As-containing compound in a serine esterase active site and the first example of covalent modification of serine by arsenic. Thus, the HerE complex reveals the structural basis for the broad scope inhibition of serine hydrolases by As(V)-containing organic compounds. | ||
- | |||
- | Observation of an arsenic adduct in an acetyl esterase crystal structure.,Zhu X, Larsen NA, Basran A, Bruce NC, Wilson IA J Biol Chem. 2003 Jan 17;278(3):2008-14. Epub 2002 Nov 5. PMID:12421810<ref>PMID:12421810</ref> | ||
- | |||
- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 1lzl" style="background-color:#fffaf0;"></div> | ||
- | == References == | ||
- | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: | + | [[Category: Rhodococcus sp]] |
- | [[Category: Basran | + | [[Category: Basran A]] |
- | [[Category: Bruce | + | [[Category: Bruce NC]] |
- | [[Category: Larsen | + | [[Category: Larsen NA]] |
- | [[Category: Wilson | + | [[Category: Wilson IA]] |
- | [[Category: Zhu | + | [[Category: Zhu X]] |
- | + | ||
- | + |
Current revision
Bacterial Heroin Esterase
|
Categories: Large Structures | Rhodococcus sp | Basran A | Bruce NC | Larsen NA | Wilson IA | Zhu X