2gvq

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[[Image:2gvq.gif|left|200px]]
 
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==Anthranilate phosphoribosyl-transferase (TRPD) from S. solfataricus in complex with anthranilate==
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The line below this paragraph, containing "STRUCTURE_2gvq", creates the "Structure Box" on the page.
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<StructureSection load='2gvq' size='340' side='right'caption='[[2gvq]], [[Resolution|resolution]] 2.43&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2gvq]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus Saccharolobus solfataricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GVQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GVQ FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.43&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BE2:2-AMINOBENZOIC+ACID'>BE2</scene></td></tr>
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{{STRUCTURE_2gvq| PDB=2gvq | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2gvq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gvq OCA], [https://pdbe.org/2gvq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gvq RCSB], [https://www.ebi.ac.uk/pdbsum/2gvq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gvq ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/TRPD_SACS2 TRPD_SACS2] Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).[HAMAP-Rule:MF_00211]<ref>PMID:11298741</ref> <ref>PMID:16714288</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gv/2gvq_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2gvq ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The metabolic synthesis and degradation of essential nucleotide compounds are primarily carried out by phosphoribosyltransferases (PRT) and nucleoside phosphorylases (NP), respectively. Despite the resemblance of their reactions, five classes of PRTs and NPs exist, where anthranilate PRT (AnPRT) constitutes the only evolutionary link between synthesis and degradation processes. We have characterized the active site of dimeric AnPRT from Sulfolobus solfataricus by elucidating crystal structures of the wild-type enzyme complexed to its two natural substrates anthranilate and 5-phosphoribosyl-1-pyrophosphate/Mg(2+). These bind into two different domains within each protomer and are brought together during catalysis by rotational domain motions as shown by small angle x-ray scattering data. Steady-state kinetics of mutated AnPRT variants address the role of active site residues in binding and catalysis. Results allow the comparative analysis of PRT and pyrimidine NP families and expose related structural motifs involved in nucleotide/nucleoside recognition by these enzyme families.
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'''Anthranilate phosphoribosyl-transferase (TRPD) from S. solfataricus in complex with anthranilate'''
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Structural and mutational analysis of substrate complexation by anthranilate phosphoribosyltransferase from Sulfolobus solfataricus.,Marino M, Deuss M, Svergun DI, Konarev PV, Sterner R, Mayans O J Biol Chem. 2006 Jul 28;281(30):21410-21. Epub 2006 May 19. PMID:16714288<ref>PMID:16714288</ref>
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==Overview==
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The metabolic synthesis and degradation of essential nucleotide compounds are primarily carried out by phosphoribosyltransferases (PRT) and nucleoside phosphorylases (NP), respectively. Despite the resemblance of their reactions, five classes of PRTs and NPs exist, where anthranilate PRT (AnPRT) constitutes the only evolutionary link between synthesis and degradation processes. We have characterized the active site of dimeric AnPRT from Sulfolobus solfataricus by elucidating crystal structures of the wild-type enzyme complexed to its two natural substrates anthranilate and 5-phosphoribosyl-1-pyrophosphate/Mg(2+). These bind into two different domains within each protomer and are brought together during catalysis by rotational domain motions as shown by small angle x-ray scattering data. Steady-state kinetics of mutated AnPRT variants address the role of active site residues in binding and catalysis. Results allow the comparative analysis of PRT and pyrimidine NP families and expose related structural motifs involved in nucleotide/nucleoside recognition by these enzyme families.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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2GVQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_solfataricus Sulfolobus solfataricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GVQ OCA].
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</div>
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<div class="pdbe-citations 2gvq" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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Structural and mutational analysis of substrate complexation by anthranilate phosphoribosyltransferase from Sulfolobus solfataricus., Marino M, Deuss M, Svergun DI, Konarev PV, Sterner R, Mayans O, J Biol Chem. 2006 Jul 28;281(30):21410-21. Epub 2006 May 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16714288 16714288]
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*[[Phosphoribosyltransferase 3D structures|Phosphoribosyltransferase 3D structures]]
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[[Category: Anthranilate phosphoribosyltransferase]]
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== References ==
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[[Category: Single protein]]
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<references/>
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[[Category: Sulfolobus solfataricus]]
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__TOC__
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[[Category: Deuss, M.]]
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</StructureSection>
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[[Category: Marino, M.]]
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[[Category: Large Structures]]
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[[Category: Mayans, O.]]
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[[Category: Saccharolobus solfataricus]]
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[[Category: Sterner, R.]]
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[[Category: Deuss M]]
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[[Category: Protein-ligand complex]]
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[[Category: Marino M]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:35:49 2008''
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[[Category: Mayans O]]
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[[Category: Sterner R]]

Current revision

Anthranilate phosphoribosyl-transferase (TRPD) from S. solfataricus in complex with anthranilate

PDB ID 2gvq

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