3c2o

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(New page: 200px {{Structure |PDB= 3c2o |SIZE=350|CAPTION= <scene name='initialview01'>3c2o</scene>, resolution 2.300&Aring; |SITE= <scene name='pdbsite=AC1:Ntm+Binding+Site...)
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|GENE= BNA6, QPT1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
|GENE= BNA6, QPT1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=cd01572 QPRTase], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=COG0157 NadC]</span>
|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=cd01572 QPRTase], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=COG0157 NadC]</span>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3c2o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c2o OCA], [http://www.ebi.ac.uk/pdbsum/3c2o PDBsum], [http://www.fli-leibniz.de/cgi-bin/ImgLib.pl?CODE=1kfv JenaLib], [http://www.rcsb.org/pdb/explore.do?structureId=3c2o RCSB]</span>
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|RELATEDENTRY=[[3c2d|3C2D]], [[3c2e|3C2E]], [[3c2f|3C2F]], [[3c2r|3C2R]], [[3c2v|3C2V]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3c2o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c2o OCA], [http://www.ebi.ac.uk/pdbsum/3c2o PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3c2o RCSB]</span>
}}
}}
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[[Category: x-ray structure]]
[[Category: x-ray structure]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 26 09:57:40 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:30:18 2008''

Revision as of 02:30, 31 March 2008

Image:3c2o.jpg


PDB ID 3c2o

Drag the structure with the mouse to rotate
, resolution 2.300Å
Sites:
Ligands:
Gene: BNA6, QPT1 (Saccharomyces cerevisiae)
Activity: Nicotinate-nucleotide diphosphorylase (carboxylating), with EC number 2.4.2.19
Domains: QPRTase, NadC
Related: 3C2D, 3C2E, 3C2F, 3C2R, 3C2V


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Crystal structure of the quinolinate phosphoribosyl transferase (BNA6) from Sachharomyces cerevisiae complexed with quinolinate


Overview

Quinolinic acid phosphoribosyl transferase (QAPRTase, EC 2.4.2.19) is a 32 kDa enzyme encoded by the BNA6 gene in yeast and catalyzes the formation of nicotinate mononucleotide from quinolinate and 5-phosphoribosyl-1-pyrophosphate (PRPP). QAPRTase plays a key role in the tryptophan degradation pathway via kynurenine, leading to the de novo biosynthesis of NAD (+) and clearing the neurotoxin quinolinate. To improve our understanding of the specificity of the eukaryotic enzyme and the course of events associated with catalysis, we have determined the crystal structures of the apo and singly bound forms with the substrates quinolinate and PRPP. This reveals that the enzyme folds in a manner similar to that of various prokaryotic forms which are approximately 30% identical in sequence. In addition, the structure of the Michaelis complex is approximated by PRPP and the quinolinate analogue phthalate bound to the active site. These results allow insight into the kinetic mechanism of QAPRTase and provide an understanding of structural diversity in the active site of the Saccharomyces cerevisiae enzyme when compared to prokaryotic homologues.

About this Structure

3C2O is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Comprehensive X-ray Structural Studies of the Quinolinate Phosphoribosyl Transferase (BNA6) from Saccharomyces cerevisiae., di Luccio E, Wilson DK, Biochemistry. 2008 Apr 1;47(13):4039-50. Epub 2008 Mar 6. PMID:18321072

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