1nul: Difference between revisions

Revision as of 15:10, 21 February 2008

XPRTASE FROM E. COLI

OverviewOverview

Xanthine phosphoribosyltransferase (XPRT; EC 2.4.2.22) from Escherichia coli is a tetrameric enzyme having 152 residues per subunit. XPRT catalyzes the transfer of the phosphoribosyl group from 5-phospho-alpha-D-ribosyl 1-pyrophosphate (PRib-PP) to the 6-oxopurine bases guanine, xanthine, and hypoxanthine to form GMP, XMP, and IMP, respectively. Crystals grown in the absence of substrate or product were used to determine the structure of XPRT at a resolution of 1.8 A, by multiple isomorphous replacement. The core structure of XPRT includes a five-stranded parallel beta-sheet surrounded by three alpha-helices, which is similar to that observed in other known phosphoribosyltransferase (PRTase) structures. The XPRT structure also has several interesting features. A glutamine residue in the purine binding site may be responsible for the altered 6-oxopurine base specificity seen in this enzyme compared to other 6-oxopurine PRTases. Also, we observe both a magnesium ion and a sulfate ion bound at the PRib-PP binding site of XPRT. The sulfate ion interacts with Arg-37 which has a cis-peptide conformation, and the magnesium ion interacts with Asp-89, a highly conserved acidic residue in the PRib-PP binding site motif. The XPRT structure also incorporates a feature which has not been observed in other PRTase structures. The C-terminal 12 residues of XPRT adopt an unusual extended conformation and make interactions with a neighboring subunit. The very last residue, Arg-152, could form part of the active site of a symmetry-related subunit in the XPRT tetramer.

About this StructureAbout this Structure

1NUL is a Single protein structure of sequence from Escherichia coli with and as ligands. Active as Xanthine phosphoribosyltransferase, with EC number 2.4.2.22 Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of Escherichia coli xanthine phosphoribosyltransferase., Vos S, de Jersey J, Martin JL, Biochemistry. 1997 Apr 8;36(14):4125-34. PMID:9100006

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 '''XPRTASE FROM E. COLI'''<br />
 ==Overview==
-Xanthine phosphoribosyltransferase (XPRT; EC 2.4.2.22) from Escherichia, coli is a tetrameric enzyme having 152 residues per subunit. XPRT, catalyzes the transfer of the phosphoribosyl group from, 5-phospho-alpha-D-ribosyl 1-pyrophosphate (PRib-PP) to the 6-oxopurine, bases guanine, xanthine, and hypoxanthine to form GMP, XMP, and IMP, respectively. Crystals grown in the absence of substrate or product were, used to determine the structure of XPRT at a resolution of 1.8 A, by, multiple isomorphous replacement. The core structure of XPRT includes a, five-stranded parallel beta-sheet surrounded by three alpha-helices, which, is similar to that observed in other known phosphoribosyltransferase, (PRTase) structures. The XPRT structure also has several interesting, features. A glutamine residue in the purine binding site may be, responsible for the altered 6-oxopurine base specificity seen in this, enzyme compared to other 6-oxopurine PRTases. Also, we observe both a, magnesium ion and a sulfate ion bound at the PRib-PP binding site of XPRT., The sulfate ion interacts with Arg-37 which has a cis-peptide, conformation, and the magnesium ion interacts with Asp-89, a highly, conserved acidic residue in the PRib-PP binding site motif. The XPRT, structure also incorporates a feature which has not been observed in other, PRTase structures. The C-terminal 12 residues of XPRT adopt an unusual, extended conformation and make interactions with a neighboring subunit., The very last residue, Arg-152, could form part of the active site of a, symmetry-related subunit in the XPRT tetramer.
+Xanthine phosphoribosyltransferase (XPRT; EC 2.4.2.22) from Escherichia coli is a tetrameric enzyme having 152 residues per subunit. XPRT catalyzes the transfer of the phosphoribosyl group from 5-phospho-alpha-D-ribosyl 1-pyrophosphate (PRib-PP) to the 6-oxopurine bases guanine, xanthine, and hypoxanthine to form GMP, XMP, and IMP, respectively. Crystals grown in the absence of substrate or product were used to determine the structure of XPRT at a resolution of 1.8 A, by multiple isomorphous replacement. The core structure of XPRT includes a five-stranded parallel beta-sheet surrounded by three alpha-helices, which is similar to that observed in other known phosphoribosyltransferase (PRTase) structures. The XPRT structure also has several interesting features. A glutamine residue in the purine binding site may be responsible for the altered 6-oxopurine base specificity seen in this enzyme compared to other 6-oxopurine PRTases. Also, we observe both a magnesium ion and a sulfate ion bound at the PRib-PP binding site of XPRT. The sulfate ion interacts with Arg-37 which has a cis-peptide conformation, and the magnesium ion interacts with Asp-89, a highly conserved acidic residue in the PRib-PP binding site motif. The XPRT structure also incorporates a feature which has not been observed in other PRTase structures. The C-terminal 12 residues of XPRT adopt an unusual extended conformation and make interactions with a neighboring subunit. The very last residue, Arg-152, could form part of the active site of a symmetry-related subunit in the XPRT tetramer.
 ==About this Structure==
-NUL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with SO4 and MG as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Xanthine_phosphoribosyltransferase Xanthine phosphoribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.22 2.4.2.22] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NUL OCA].
+NUL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Xanthine_phosphoribosyltransferase Xanthine phosphoribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.22 2.4.2.22] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NUL OCA].
 ==Reference==
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 [[Category: Single protein]]
 [[Category: Xanthine phosphoribosyltransferase]]
-[[Category: Jersey, J.De.]]
+[[Category: Jersey, J De.]]
-[[Category: Martin, J.L.]]
+[[Category: Martin, J L.]]
 [[Category: Vos, S.]]
 [[Category: MG]]
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 [[Category: transferase]]
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