2ji8: Difference between revisions

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==About this Structure==
==About this Structure==
2JI8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oxalobacter_formigenes Oxalobacter formigenes] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=TPP:'>TPP</scene>, <scene name='pdbligand=ADP:'>ADP</scene>, <scene name='pdbligand=FYN:'>FYN</scene> and <scene name='pdbligand=PGE:'>PGE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Oxalyl-CoA_decarboxylase Oxalyl-CoA decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.8 4.1.1.8] Known structural/functional Site: <scene name='pdbsite=AC1:Pge Binding Site For Chain B'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JI8 OCA].  
2JI8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oxalobacter_formigenes Oxalobacter formigenes] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=TPP:'>TPP</scene>, <scene name='pdbligand=ADP:'>ADP</scene>, <scene name='pdbligand=FYN:'>FYN</scene> and <scene name='pdbligand=PGE:'>PGE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Oxalyl-CoA_decarboxylase Oxalyl-CoA decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.8 4.1.1.8] Known structural/functional Site: <scene name='pdbsite=AC1:Pge+Binding+Site+For+Chain+B'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JI8 OCA].  


==Reference==
==Reference==
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[[Category: thiamine pyrophosphate]]
[[Category: thiamine pyrophosphate]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 10:46:10 2008''

Revision as of 11:46, 3 February 2008

File:2ji8.jpg


2ji8, resolution 2.15Å

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X-RAY STRUCTURE OF OXALYL-COA DECARBOXYLASE IN COMPLEX WITH FORMYL-COA

OverviewOverview

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.

About this StructureAbout this Structure

2JI8 is a Single protein structure of sequence from Oxalobacter formigenes with , , , and as ligands. Active as Oxalyl-CoA decarboxylase, with EC number 4.1.1.8 Known structural/functional Site: . Full crystallographic information is available from OCA.

ReferenceReference

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

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