1zyk
From Proteopedia
(New page: 200px<br /><applet load="1zyk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zyk, resolution 2.4Å" /> '''Anthranilate Phosphor...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1zyk.gif|left|200px]]<br /><applet load="1zyk" size=" | + | [[Image:1zyk.gif|left|200px]]<br /><applet load="1zyk" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1zyk, resolution 2.4Å" /> | caption="1zyk, resolution 2.4Å" /> | ||
'''Anthranilate Phosphoribosyltransferase in complex with PRPP, anthranilate and magnesium'''<br /> | '''Anthranilate Phosphoribosyltransferase in complex with PRPP, anthranilate and magnesium'''<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== | ||
| - | 1ZYK 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, PRP and BE2 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:// | + | 1ZYK 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>, <scene name='pdbligand=PRP:'>PRP</scene> and <scene name='pdbligand=BE2:'>BE2</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=1ZYK OCA]. |
==Reference== | ==Reference== | ||
| Line 26: | Line 26: | ||
[[Category: trpd]] | [[Category: trpd]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:20:20 2008'' |
Revision as of 14:20, 21 February 2008
|
Anthranilate Phosphoribosyltransferase in complex with PRPP, anthranilate and magnesium
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
1ZYK 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.
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 Thu Feb 21 16:20:20 2008
