1zxy: Difference between revisions

Revision as of 17:20, 21 February 2008

Anthranilate Phosphoribosyltransferase from Sulfolobus solfataricus in complex with PRPP and Magnesium

OverviewOverview

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 StructureAbout this Structure

1ZXY is a Single protein structure of sequence from Sulfolobus solfataricus with and as ligands. Active as Anthranilate phosphoribosyltransferase, with EC number 2.4.2.18 Full crystallographic information is available from OCA.

ReferenceReference

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 Thu Feb 21 16:20:10 2008

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OCA

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 '''Anthranilate Phosphoribosyltransferase from Sulfolobus solfataricus in complex with PRPP and Magnesium'''<br />
 ==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.
+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==
-ZXY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_solfataricus Sulfolobus solfataricus] with MG and PRP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ZXY OCA].
+ZXY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_solfataricus Sulfolobus solfataricus] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=PRP:'>PRP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZXY OCA].
 ==Reference==
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 [[Category: trpd]]
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