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2jib

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Revision as of 10:01, 30 April 2014

X-RAY STRUCTURE OF OXALYL-COA DECARBOXYLASE IN COMPLEX WITH COENZYME-A

Structural highlights

2jib is a 2 chain structure with sequence from Oxalobacter formigenes. Full crystallographic information is available from OCA.
Ligands: , , , ,
Related: 2c31, 2ji6, 2ji7, 2ji8, 2ji9
Activity: Glucokinase, with EC number 2.7.1.2
Resources: FirstGlance, OCA, RCSB, PDBsum

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 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^[1]

From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.

References

↑ Berthold CL, Toyota CG, Moussatche P, Wood MD, Leeper F, Richards NG, Lindqvist Y. Crystallographic snapshots of oxalyl-CoA decarboxylase give insights into catalysis by nonoxidative ThDP-dependent decarboxylases. Structure. 2007 Jul;15(7):853-61. PMID:17637344 doi:http://dx.doi.org/10.1016/j.str.2007.06.001

1 Structural highlights
2 Evolutionary Conservation
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2jib"

@@ Line 3: / Line 3: @@
 == Structural highlights ==
 [[2jib]] 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=2JIB OCA]. <br>
-<b>Related:</b> [[2c31|2c31]], [[2ji6|2ji6]], [[2ji7|2ji7]], [[2ji8|2ji8]], [[2ji9|2ji9]]<br>
+<b>[[Ligand|Ligands:]]</b> <scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene><br>
+<b>[[Related_structure|Related:]]</b> [[2c31|2c31]], [[2ji6|2ji6]], [[2ji7|2ji7]], [[2ji8|2ji8]], [[2ji9|2ji9]]<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>
+<b>Resources:</b> <span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2jib FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jib OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2jib RCSB], [http://www.ebi.ac.uk/pdbsum/2jib PDBsum]</span><br>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|right]]

2jib

From Proteopedia

Revision as of 10:01, 30 April 2014

X-RAY STRUCTURE OF OXALYL-COA DECARBOXYLASE IN COMPLEX WITH COENZYME-A

Structural highlights

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

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