2gvq
From Proteopedia
(New page: 200px<br /><applet load="2gvq" size="450" color="white" frame="true" align="right" spinBox="true" caption="2gvq, resolution 2.43Å" /> '''Anthranilate phospho...) |
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| - | [[Image:2gvq.gif|left|200px]]<br /><applet load="2gvq" size=" | + | [[Image:2gvq.gif|left|200px]]<br /><applet load="2gvq" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2gvq, resolution 2.43Å" /> | caption="2gvq, resolution 2.43Å" /> | ||
'''Anthranilate phosphoribosyl-transferase (TRPD) from S. solfataricus in complex with anthranilate'''<br /> | '''Anthranilate phosphoribosyl-transferase (TRPD) from S. solfataricus in complex with anthranilate'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The metabolic synthesis and degradation of essential nucleotide compounds | + | 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== | ==About this Structure== | ||
| - | 2GVQ 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 BE2 as [http://en.wikipedia.org/wiki/ligand ligand]. 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:// | + | 2GVQ 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=BE2:'>BE2</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=2GVQ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: protein-ligand complex]] | [[Category: protein-ligand complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:35:52 2008'' |
Revision as of 15:35, 21 February 2008
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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 with as ligand. Active as Anthranilate phosphoribosyltransferase, with EC number 2.4.2.18 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
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