2jbm

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[[Image:2jbm.jpg|left|200px]]
[[Image:2jbm.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 2jbm |SIZE=350|CAPTION= <scene name='initialview01'>2jbm</scene>, resolution 2.00&Aring;
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The line below this paragraph, containing "STRUCTURE_2jbm", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=AC1:Srt+Binding+Site+For+Chain+A'>AC1</scene>, <scene name='pdbsite=AC2:Srt+Binding+Site+For+Chain+B'>AC2</scene>, <scene name='pdbsite=AC3:Srt+Binding+Site+For+Chain+C'>AC3</scene>, <scene name='pdbsite=AC4:Srt+Binding+Site+For+Chain+D'>AC4</scene>, <scene name='pdbsite=AC5:Srt+Binding+Site+For+Chain+E'>AC5</scene>, <scene name='pdbsite=AC6:Srt+Binding+Site+For+Chain+F'>AC6</scene>, <scene name='pdbsite=AC7:Srt+Binding+Site+For+Chain+G'>AC7</scene>, <scene name='pdbsite=AC8:Srt+Binding+Site+For+Chain+H'>AC8</scene>, <scene name='pdbsite=AC9:Srt+Binding+Site+For+Chain+I'>AC9</scene>, <scene name='pdbsite=BC1:Srt+Binding+Site+For+Chain+J'>BC1</scene>, <scene name='pdbsite=BC2:Srt+Binding+Site+For+Chain+K'>BC2</scene> and <scene name='pdbsite=BC3:Srt+Binding+Site+For+Chain+L'>BC3</scene>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=SRT:S,R+MESO-TARTARIC+ACID'>SRT</scene>
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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=
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-->
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|DOMAIN=
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{{STRUCTURE_2jbm| PDB=2jbm | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2jbm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jbm OCA], [http://www.ebi.ac.uk/pdbsum/2jbm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2jbm RCSB]</span>
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}}
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'''QPRTASE STRUCTURE FROM HUMAN'''
'''QPRTASE STRUCTURE FROM HUMAN'''
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Structural and kinetic characterization of quinolinate phosphoribosyltransferase (hQPRTase) from homo sapiens., Liu H, Woznica K, Catton G, Crawford A, Botting N, Naismith JH, J Mol Biol. 2007 Oct 26;373(3):755-63. Epub 2007 Aug 24. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17868694 17868694]
Structural and kinetic characterization of quinolinate phosphoribosyltransferase (hQPRTase) from homo sapiens., Liu H, Woznica K, Catton G, Crawford A, Botting N, Naismith JH, J Mol Biol. 2007 Oct 26;373(3):755-63. Epub 2007 Aug 24. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17868694 17868694]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Nicotinate-nucleotide diphosphorylase (carboxylating)]]
 
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Liu, H.]]
[[Category: Liu, H.]]
[[Category: Naismith, J H.]]
[[Category: Naismith, J H.]]
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[[Category: enzyme]]
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[[Category: Enzyme]]
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[[Category: glycosyltransferase]]
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[[Category: Glycosyltransferase]]
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[[Category: metabolism]]
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[[Category: Metabolism]]
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[[Category: nad]]
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[[Category: Nad]]
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[[Category: polymorphism]]
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[[Category: Polymorphism]]
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[[Category: pyridine nucleotide biosynthesis]]
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[[Category: Pyridine nucleotide biosynthesis]]
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[[Category: transferase]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 08:39:09 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:55:51 2008''
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Revision as of 05:39, 4 May 2008

Image:2jbm.jpg

Template:STRUCTURE 2jbm

QPRTASE STRUCTURE FROM HUMAN


Overview

Human quinolinate phosphoribosyltransferase (EC 2.4.2.19) (hQPRTase) is a member of the type II phosphoribosyltransferase family involved in the catabolism of quinolinic acid (QA). It catalyses the formation of nicotinic acid mononucleotide from quinolinic acid, which involves a phosphoribosyl transfer reaction followed by decarboxylation. hQPRTase has been implicated in a number of neurological conditions and in order to study it further, we have carried out structural and kinetic studies on recombinant hQPRTase. The structure of the fully active enzyme overexpressed in Escherichia coli was solved using multiwavelength methods to a resolution of 2.0 A. hQPRTase has a alpha/beta barrel fold sharing a similar overall structure with the bacterial QPRTases. The active site of hQPRTase is located at an alpha/beta open sandwich structure that serves as a cup for the alpha/beta barrel of the adjacent subunit with a QA binding site consisting of three arginine residues (R102, R138 and R161) and two lysine residues (K139 and K171). Mutation of these residues affected substrate binding or abolished the enzymatic activity. The kinetics of the human enzyme are different to the bacterial enzymes studied, hQPRTase is inhibited competitively and non-competitively by one of its substrates, 5-phosphoribosylpyrophosphate (PRPP). The human enzyme adopts a hexameric arrangement, which places the active sites in close proximity to each other.

About this Structure

2JBM is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural and kinetic characterization of quinolinate phosphoribosyltransferase (hQPRTase) from homo sapiens., Liu H, Woznica K, Catton G, Crawford A, Botting N, Naismith JH, J Mol Biol. 2007 Oct 26;373(3):755-63. Epub 2007 Aug 24. PMID:17868694 Page seeded by OCA on Sun May 4 08:39:09 2008

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