2gvq

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[[Image:2gvq.gif|left|200px]]
[[Image:2gvq.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 2gvq |SIZE=350|CAPTION= <scene name='initialview01'>2gvq</scene>, resolution 2.43&Aring;
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The line below this paragraph, containing "STRUCTURE_2gvq", 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= <scene name='pdbligand=BE2:2-AMINOBENZOIC+ACID'>BE2</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/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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or leave the SCENE parameter empty for the default display.
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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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-->
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|DOMAIN=
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{{STRUCTURE_2gvq| PDB=2gvq | SCENE= }}
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|RELATEDENTRY=[[1o17|1O17]], [[1gxb|1GXB]], [[1zxy|1ZXY]], [[1zyk|1ZYK]]
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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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}}
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'''Anthranilate phosphoribosyl-transferase (TRPD) from S. solfataricus in complex with anthranilate'''
'''Anthranilate phosphoribosyl-transferase (TRPD) from S. solfataricus in complex with anthranilate'''
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[[Category: Mayans, O.]]
[[Category: Mayans, O.]]
[[Category: Sterner, R.]]
[[Category: Sterner, R.]]
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[[Category: protein-ligand complex]]
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[[Category: Protein-ligand complex]]
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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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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:22:18 2008''
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Revision as of 02:35, 4 May 2008

Image:2gvq.gif

Template:STRUCTURE 2gvq

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


Overview

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.

About this Structure

2GVQ is a Single protein structure of sequence from Sulfolobus solfataricus. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Sun May 4 05:35:49 2008

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