2jbm

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:36, 9 May 2024) (edit) (undo)
 
(11 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2jbm.jpg|left|200px]]
 
-
{{Structure
+
==QPRTASE STRUCTURE FROM HUMAN==
-
|PDB= 2jbm |SIZE=350|CAPTION= <scene name='initialview01'>2jbm</scene>, resolution 2.00&Aring;
+
<StructureSection load='2jbm' size='340' side='right'caption='[[2jbm]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
-
|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>
+
== Structural highlights ==
-
|LIGAND= <scene name='pdbligand=SRT:S,R+MESO-TARTARIC+ACID'>SRT</scene>
+
<table><tr><td colspan='2'>[[2jbm]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JBM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JBM FirstGlance]. <br>
-
|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>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
-
|GENE=
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SRT:S,R+MESO-TARTARIC+ACID'>SRT</scene></td></tr>
-
|DOMAIN=
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2jbm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jbm OCA], [https://pdbe.org/2jbm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jbm RCSB], [https://www.ebi.ac.uk/pdbsum/2jbm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jbm ProSAT]</span></td></tr>
-
|RELATEDENTRY=
+
</table>
-
|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>
+
== Function ==
-
}}
+
[https://www.uniprot.org/uniprot/NADC_HUMAN NADC_HUMAN] Involved in the catabolism of quinolinic acid (QA).<ref>PMID:17868694</ref>
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jb/2jbm_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2jbm ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
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.
-
'''QPRTASE STRUCTURE FROM HUMAN'''
+
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<ref>PMID:17868694</ref>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 2jbm" style="background-color:#fffaf0;"></div>
-
==Overview==
+
==See Also==
-
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.
+
*[[Phosphoribosyltransferase 3D structures|Phosphoribosyltransferase 3D structures]]
-
 
+
== References ==
-
==About this Structure==
+
<references/>
-
2JBM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JBM OCA].
+
__TOC__
-
 
+
</StructureSection>
-
==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:[http://www.ncbi.nlm.nih.gov/pubmed/17868694 17868694]
+
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Nicotinate-nucleotide diphosphorylase (carboxylating)]]
+
[[Category: Large Structures]]
-
[[Category: Single protein]]
+
[[Category: Liu H]]
-
[[Category: Liu, H.]]
+
[[Category: Naismith JH]]
-
[[Category: Naismith, J H.]]
+
-
[[Category: enzyme]]
+
-
[[Category: glycosyltransferase]]
+
-
[[Category: metabolism]]
+
-
[[Category: nad]]
+
-
[[Category: polymorphism]]
+
-
[[Category: pyridine nucleotide biosynthesis]]
+
-
[[Category: transferase]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:55:51 2008''
+

Current revision

QPRTASE STRUCTURE FROM HUMAN

PDB ID 2jbm

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2jbm"
Personal tools