2gvq

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[[Image:2gvq.gif|left|200px]]
 
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{{Structure
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==Anthranilate phosphoribosyl-transferase (TRPD) from S. solfataricus in complex with anthranilate==
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|PDB= 2gvq |SIZE=350|CAPTION= <scene name='initialview01'>2gvq</scene>, resolution 2.43&Aring;
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<StructureSection load='2gvq' size='340' side='right'caption='[[2gvq]], [[Resolution|resolution]] 2.43&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=BE2:2-AMINOBENZOIC+ACID'>BE2</scene>
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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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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Anthranilate_phosphoribosyltransferase Anthranilate phosphoribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.18 2.4.2.18] </span>
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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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|GENE= TRPD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2287 Sulfolobus solfataricus])
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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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|DOMAIN=
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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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|RELATEDENTRY=[[1o17|1O17]], [[1gxb|1GXB]], [[1zxy|1ZXY]], [[1zyk|1ZYK]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2gvq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gvq OCA], [http://www.ebi.ac.uk/pdbsum/2gvq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2gvq RCSB]</span>
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== Function ==
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}}
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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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'''Anthranilate phosphoribosyl-transferase (TRPD) from S. solfataricus in complex with anthranilate'''
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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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==Overview==
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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 ==
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.
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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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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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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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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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</div>
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[[Category: Anthranilate phosphoribosyltransferase]]
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<div class="pdbe-citations 2gvq" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Sulfolobus solfataricus]]
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[[Category: Deuss, M.]]
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[[Category: Marino, M.]]
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[[Category: Mayans, O.]]
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[[Category: Sterner, R.]]
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[[Category: protein-ligand complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:22:18 2008''
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==See Also==
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*[[Phosphoribosyltransferase 3D structures|Phosphoribosyltransferase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Saccharolobus solfataricus]]
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[[Category: Deuss M]]
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[[Category: Marino M]]
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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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