1esc
From Proteopedia
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- | [[Image:1esc.png|left|200px]] | ||
- | + | ==THE MOLECULAR MECHANISM OF ENANTIORECOGNITION BY ESTERASES== | |
+ | <StructureSection load='1esc' size='340' side='right'caption='[[1esc]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[1esc]] 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=1ESC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ESC FirstGlance]. <br> | ||
+ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</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=1esc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1esc OCA], [https://pdbe.org/1esc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1esc RCSB], [https://www.ebi.ac.uk/pdbsum/1esc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1esc ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/ESTA_STRSC ESTA_STRSC] | ||
+ | == Evolutionary Conservation == | ||
+ | [[Image:Consurf_key_small.gif|200px|right]] | ||
+ | Check<jmol> | ||
+ | <jmolCheckbox> | ||
+ | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/es/1esc_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
+ | <text>to colour the structure by Evolutionary Conservation</text> | ||
+ | </jmolCheckbox> | ||
+ | </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=1esc ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | 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. | ||
- | + | 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> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | <div class="pdbe-citations 1esc" style="background-color:#fffaf0;"></div> | |
- | + | == References == | |
- | == | + | <references/> |
- | < | + | __TOC__ |
+ | </StructureSection> | ||
+ | [[Category: Large Structures]] | ||
[[Category: Streptomyces scabiei]] | [[Category: Streptomyces scabiei]] | ||
- | [[Category: Derewenda | + | [[Category: Derewenda U]] |
- | [[Category: Derewenda | + | [[Category: Derewenda ZS]] |
- | [[Category: Patkar | + | [[Category: Patkar S]] |
- | [[Category: Schottel | + | [[Category: Schottel JL]] |
- | [[Category: Swenson | + | [[Category: Swenson L]] |
- | [[Category: Wei | + | [[Category: Wei Y]] |
Current revision
THE MOLECULAR MECHANISM OF ENANTIORECOGNITION BY ESTERASES
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