2ji7
From Proteopedia
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- | [[Image: | + | ==X-RAY STRUCTURE OF OXALYL-COA DECARBOXYLASE WITH COVALENT REACTION INTERMEDIATE== |
+ | <StructureSection load='2ji7' size='340' side='right' caption='[[2ji7]], [[Resolution|resolution]] 1.82Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | [[2ji7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Oxalobacter_formigenes Oxalobacter formigenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JI7 OCA]. <br> | ||
+ | <b>Related:</b> [[2c31|2c31]], [[2ji6|2ji6]], [[2ji8|2ji8]], [[2ji9|2ji9]], [[2jib|2jib]]<br> | ||
+ | <b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br> | ||
+ | == Evolutionary Conservation == | ||
+ | [[Image:Consurf_key_small.gif|right]] | ||
+ | Check<jmol> | ||
+ | <jmolCheckbox> | ||
+ | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ji/2ji7_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> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Despite more than five decades of extensive studies of thiamin diphosphate (ThDP) enzymes, there remain many uncertainties as to how these enzymes achieve their rate enhancements. Here, we present a clear picture of catalysis for the simple nonoxidative decarboxylase, oxalyl-coenzyme A (CoA) decarboxylase, based on crystallographic snapshots along the catalytic cycle and kinetic data on active site mutants. First, we provide crystallographic evidence that, upon binding of oxalyl-CoA, the C-terminal 13 residues fold over the substrate, aligning the substrate alpha-carbon for attack by the ThDP-C2 atom. The second structure presented shows a covalent reaction intermediate after decarboxylation, interpreted as being nonplanar. Finally, the structure of a product complex is presented. In accordance with mutagenesis data, no side chains of the enzyme are implied to directly participate in proton transfer except the glutamic acid (Glu-56), which promotes formation of the 1',4'-iminopyrimidine tautomer of ThDP needed for activation. | ||
- | + | Crystallographic snapshots of oxalyl-CoA decarboxylase give insights into catalysis by nonoxidative ThDP-dependent decarboxylases.,Berthold CL, Toyota CG, Moussatche P, Wood MD, Leeper F, Richards NG, Lindqvist Y Structure. 2007 Jul;15(7):853-61. PMID:17637344<ref>PMID:17637344</ref> | |
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- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | + | </StructureSection> | |
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[[Category: Oxalobacter formigenes]] | [[Category: Oxalobacter formigenes]] | ||
[[Category: Oxalyl-CoA decarboxylase]] | [[Category: Oxalyl-CoA decarboxylase]] |
Revision as of 08:20, 30 April 2014
X-RAY STRUCTURE OF OXALYL-COA DECARBOXYLASE WITH COVALENT REACTION INTERMEDIATE
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Categories: Oxalobacter formigenes | Oxalyl-CoA decarboxylase | Berthold, C L. | Leeper, F. | Lindqvist, Y. | Moussatche, P. | Richards, N G.J. | Toyota, C G. | Wood, M D. | Decarboxylase | Flavoprotein | Intermediate complex | Lyase | Non- oxidative decarboxylase | Oxalate degradation | Thiamin diphosphate-dependent | Thiamine pyrophosphate