1esc: Difference between revisions
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[[Image: | ==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 [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ESC FirstGlance]. <br> | |||
</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=1esc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1esc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1esc RCSB], [http://www.ebi.ac.uk/pdbsum/1esc PDBsum]</span></td></tr> | |||
<table> | |||
== 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/initialview01.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/chain_selection.php?pdb_ID=2ata 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> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
< | |||
[[Category: Streptomyces scabiei]] | [[Category: Streptomyces scabiei]] | ||
[[Category: Derewenda, U.]] | [[Category: Derewenda, U.]] | ||
Revision as of 14:19, 24 September 2014
THE MOLECULAR MECHANISM OF ENANTIORECOGNITION BY ESTERASESTHE MOLECULAR MECHANISM OF ENANTIORECOGNITION BY ESTERASES
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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