1esd

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(New page: 200px<br /><applet load="1esd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1esd, resolution 2.3&Aring;" /> '''THE MOLECULAR MECHANI...)
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[[Image:1esd.jpg|left|200px]]<br /><applet load="1esd" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1esd, resolution 2.3&Aring;" />
 
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'''THE MOLECULAR MECHANISM OF ENANTIORECOGNITION BY ESTERASES'''<br />
 
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==Overview==
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==THE MOLECULAR MECHANISM OF ENANTIORECOGNITION BY ESTERASES==
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The crystal structure of a novel esterase from Streptomyces scabies, a, causal agent of the potato scab disease, was solved at 2.1 A resolution., The tertiary fold of the enzyme is substantially different from that of, the alpha/beta hydrolase family and unique among all known hydrolases. The, active site contains a dyad of Ser 14 and His 283, closely resembling two, of the three components of typical Ser-His-Asp(Glu) triads from other, serine hydrolases. Proper orientation of the active site imidazol is, maintained by a hydrogen bond between the N delta-H group and a main chain, oxygen. Thus, the enzyme constitutes the first known natural variation of, the chymotrypsin-like triad in which a carboxylic acid is replaced by a, neutral hydrogen-bond acceptor.
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<StructureSection load='1esd' size='340' side='right'caption='[[1esd]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1esd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_scabiei Streptomyces scabiei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ESD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ESD FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=VXA:METHYLPHOSPHONIC+ACID+ESTER+GROUP'>VXA</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1esd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1esd OCA], [https://pdbe.org/1esd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1esd RCSB], [https://www.ebi.ac.uk/pdbsum/1esd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1esd ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ESTA_STRSC ESTA_STRSC]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/es/1esd_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1esd ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The crystal structure of a novel esterase from Streptomyces scabies, a causal agent of the potato scab disease, was solved at 2.1 A resolution. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases. The active site contains a dyad of Ser 14 and His 283, closely resembling two of the three components of typical Ser-His-Asp(Glu) triads from other serine hydrolases. Proper orientation of the active site imidazol is maintained by a hydrogen bond between the N delta-H group and a main chain oxygen. Thus, the enzyme constitutes the first known natural variation of the chymotrypsin-like triad in which a carboxylic acid is replaced by a neutral hydrogen-bond acceptor.
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==About this Structure==
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A novel variant of the catalytic triad in the Streptomyces scabies esterase.,Wei Y, Schottel JL, Derewenda U, Swenson L, Patkar S, Derewenda ZS Nat Struct Biol. 1995 Mar;2(3):218-23. PMID:7773790<ref>PMID:7773790</ref>
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1ESD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_scabiei Streptomyces scabiei] with VXA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ESD OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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A novel variant of the catalytic triad in the Streptomyces scabies esterase., Wei Y, Schottel JL, Derewenda U, Swenson L, Patkar S, Derewenda ZS, Nat Struct Biol. 1995 Mar;2(3):218-23. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7773790 7773790]
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</div>
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[[Category: Single protein]]
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<div class="pdbe-citations 1esd" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Streptomyces scabiei]]
[[Category: Streptomyces scabiei]]
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[[Category: Derewenda, U.]]
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[[Category: Derewenda U]]
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[[Category: Derewenda, Z.S.]]
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[[Category: Derewenda ZS]]
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[[Category: Patkar, S.]]
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[[Category: Patkar S]]
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[[Category: Schottel, J.L.]]
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[[Category: Schottel JL]]
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[[Category: Swenson, L.]]
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[[Category: Swenson L]]
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[[Category: Wei, Y.]]
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[[Category: Wei Y]]
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[[Category: VXA]]
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[[Category: hydrolase (serine esterase)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:16:30 2007''
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THE MOLECULAR MECHANISM OF ENANTIORECOGNITION BY ESTERASES

PDB ID 1esd

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