1grc: Difference between revisions

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[[Image:1grc.gif|left|200px]]<br /><applet load="1grc" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1grc.gif|left|200px]]<br /><applet load="1grc" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1grc, resolution 3.0Å" />

'''CRYSTAL STRUCTURE OF GLYCINAMIDE RIBONUCLEOTIDE TRANSFORMYLASE FROM ESCHERICHIA COLI AT 3.0 ANGSTROMS RESOLUTION: A TARGET ENZYME FOR CHEMOTHERAPY'''<br />

==Overview==

The atomic structure of glycinamide ribonucleotide transformylase, an, essential enzyme in purine biosynthesis, has been determined at 3.0 A, resolution. The last three C-terminal residues and a sequence stretch of, 18 residues (residues 113 to 130) are not visible in the electron density, map. The enzyme forms a dimer in the crystal structure. Each monomer is, divided into two domains, which are connected by a central mainly parallel, seven-stranded beta-sheet. The N-terminal domain contains a Rossmann type, mononucleotide fold with a phosphate ion bound to the C-terminal end of, the first beta-strand. A long narrow cleft stretches from the phosphate to, a conserved aspartic acid, Asp144, which has been suggested as an, active-site residue. The cleft is lined by a cluster of residues, which, are conserved between bacterial, yeast, avian and human enzymes, and, likely represents the binding pocket and active site of the enzyme. GAR, Tfase binds a reduced folate cofactor and glycinamide ribonucleotide for, the catalysis of one of the initial steps in purine biosynthesis. Folate, analogs and multi-substrate inhibitors of the enzyme have antineoplastic, effects and the structure determination of the unliganded enzyme and, enzyme-inhibitor complexes will aid the development of anti-cancer drugs.

The atomic structure of glycinamide ribonucleotide transformylase, an essential enzyme in purine biosynthesis, has been determined at 3.0 A resolution. The last three C-terminal residues and a sequence stretch of 18 residues (residues 113 to 130) are not visible in the electron density map. The enzyme forms a dimer in the crystal structure. Each monomer is divided into two domains, which are connected by a central mainly parallel seven-stranded beta-sheet. The N-terminal domain contains a Rossmann type mononucleotide fold with a phosphate ion bound to the C-terminal end of the first beta-strand. A long narrow cleft stretches from the phosphate to a conserved aspartic acid, Asp144, which has been suggested as an active-site residue. The cleft is lined by a cluster of residues, which are conserved between bacterial, yeast, avian and human enzymes, and likely represents the binding pocket and active site of the enzyme. GAR Tfase binds a reduced folate cofactor and glycinamide ribonucleotide for the catalysis of one of the initial steps in purine biosynthesis. Folate analogs and multi-substrate inhibitors of the enzyme have antineoplastic effects and the structure determination of the unliganded enzyme and enzyme-inhibitor complexes will aid the development of anti-cancer drugs.

==About this Structure==

1GRC 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 PO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Phosphoribosylglycinamide_formyltransferase Phosphoribosylglycinamide formyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.2.2 2.1.2.2] Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1GRC OCA].

1GRC 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=PO4:'>PO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Phosphoribosylglycinamide_formyltransferase Phosphoribosylglycinamide formyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.2.2 2.1.2.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GRC OCA].

==Reference==

Line 15:

[[Category: Single protein]]

[[Category: Chen, P.]]

[[Category: Wilson, I.A.]]

[[Category: Wilson, I A.]]

[[Category: PO4]]

[[Category: transferase(formyl)]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:53:11 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1grc.gif|left|200px]]<br /><applet load="1grc" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1grc.gif|left|200px]]<br /><applet load="1grc" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1grc, resolution 3.0&Aring;" />
 '''CRYSTAL STRUCTURE OF GLYCINAMIDE RIBONUCLEOTIDE TRANSFORMYLASE FROM ESCHERICHIA COLI AT 3.0 ANGSTROMS RESOLUTION: A TARGET ENZYME FOR CHEMOTHERAPY'''<br />
 ==Overview==
-The atomic structure of glycinamide ribonucleotide transformylase, an, essential enzyme in purine biosynthesis, has been determined at 3.0 A, resolution. The last three C-terminal residues and a sequence stretch of, 18 residues (residues 113 to 130) are not visible in the electron density, map. The enzyme forms a dimer in the crystal structure. Each monomer is, divided into two domains, which are connected by a central mainly parallel, seven-stranded beta-sheet. The N-terminal domain contains a Rossmann type, mononucleotide fold with a phosphate ion bound to the C-terminal end of, the first beta-strand. A long narrow cleft stretches from the phosphate to, a conserved aspartic acid, Asp144, which has been suggested as an, active-site residue. The cleft is lined by a cluster of residues, which, are conserved between bacterial, yeast, avian and human enzymes, and, likely represents the binding pocket and active site of the enzyme. GAR, Tfase binds a reduced folate cofactor and glycinamide ribonucleotide for, the catalysis of one of the initial steps in purine biosynthesis. Folate, analogs and multi-substrate inhibitors of the enzyme have antineoplastic, effects and the structure determination of the unliganded enzyme and, enzyme-inhibitor complexes will aid the development of anti-cancer drugs.
+The atomic structure of glycinamide ribonucleotide transformylase, an essential enzyme in purine biosynthesis, has been determined at 3.0 A resolution. The last three C-terminal residues and a sequence stretch of 18 residues (residues 113 to 130) are not visible in the electron density map. The enzyme forms a dimer in the crystal structure. Each monomer is divided into two domains, which are connected by a central mainly parallel seven-stranded beta-sheet. The N-terminal domain contains a Rossmann type mononucleotide fold with a phosphate ion bound to the C-terminal end of the first beta-strand. A long narrow cleft stretches from the phosphate to a conserved aspartic acid, Asp144, which has been suggested as an active-site residue. The cleft is lined by a cluster of residues, which are conserved between bacterial, yeast, avian and human enzymes, and likely represents the binding pocket and active site of the enzyme. GAR Tfase binds a reduced folate cofactor and glycinamide ribonucleotide for the catalysis of one of the initial steps in purine biosynthesis. Folate analogs and multi-substrate inhibitors of the enzyme have antineoplastic effects and the structure determination of the unliganded enzyme and enzyme-inhibitor complexes will aid the development of anti-cancer drugs.
 ==About this Structure==
-GRC 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 PO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Phosphoribosylglycinamide_formyltransferase Phosphoribosylglycinamide formyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.2.2 2.1.2.2] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GRC OCA].
+GRC 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=PO4:'>PO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Phosphoribosylglycinamide_formyltransferase Phosphoribosylglycinamide formyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.2.2 2.1.2.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GRC OCA].
 ==Reference==
@@ Line 15: / Line 15: @@
 [[Category: Single protein]]
 [[Category: Chen, P.]]
-[[Category: Wilson, I.A.]]
+[[Category: Wilson, I A.]]
 [[Category: PO4]]
 [[Category: transferase(formyl)]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:14:52 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:53:11 2008''