3c2e

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[[Image:3c2e.jpg|left|200px]]
[[Image:3c2e.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 3c2e |SIZE=350|CAPTION= <scene name='initialview01'>3c2e</scene>, resolution 1.900&Aring;
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The line below this paragraph, containing "STRUCTURE_3c2e", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND=
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Nicotinate-nucleotide_diphosphorylase_(carboxylating) Nicotinate-nucleotide diphosphorylase (carboxylating)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.19 2.4.2.19] </span>
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or leave the SCENE parameter empty for the default display.
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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])
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|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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{{STRUCTURE_3c2e| PDB=3c2e | SCENE= }}
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|RELATEDENTRY=[[3c2d|3C2D]], [[3c2f|3C2F]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3c2e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c2e OCA], [http://www.ebi.ac.uk/pdbsum/3c2e PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3c2e RCSB]</span>
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}}
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'''Crystal structure at 1.9A of the apo quinolinate phosphoribosyl transferase (BNA6) from Saccharomyces cerevisiae'''
'''Crystal structure at 1.9A of the apo quinolinate phosphoribosyl transferase (BNA6) from Saccharomyces cerevisiae'''
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==Reference==
==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:[http://www.ncbi.nlm.nih.gov/pubmed/18321072 18321072]
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:[http://www.ncbi.nlm.nih.gov/pubmed/18321072 18321072]
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[[Category: Nicotinate-nucleotide diphosphorylase (carboxylating)]]
 
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Luccio, E di.]]
[[Category: Luccio, E di.]]
[[Category: Wilson, D K.]]
[[Category: Wilson, D K.]]
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[[Category: bna6]]
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[[Category: Bna6]]
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[[Category: cytoplasm]]
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[[Category: Cytoplasm]]
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[[Category: glycosyltransferase]]
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[[Category: Glycosyltransferase]]
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[[Category: mechanism]]
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[[Category: Mechanism]]
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[[Category: nucleus]]
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[[Category: Nucleus]]
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[[Category: prtase]]
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[[Category: Prtase]]
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[[Category: pyridine nucleotide biosynthesis]]
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[[Category: Pyridine nucleotide biosynthesis]]
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[[Category: qprtase]]
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[[Category: Qprtase]]
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[[Category: transferase]]
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[[Category: Transferase]]
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[[Category: x-ray structure]]
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[[Category: X-ray structure]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr 24 09:34:24 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:30:21 2008''
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Revision as of 06:34, 24 April 2008

Template:STRUCTURE 3c2e

Crystal structure at 1.9A of the apo quinolinate phosphoribosyl transferase (BNA6) from Saccharomyces cerevisiae


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

3C2E 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 Page seeded by OCA on Thu Apr 24 09:34:24 2008

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