1grc

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(New page: 200px<br /><applet load="1grc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1grc, resolution 3.0&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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[[Image:1grc.gif|left|200px]]<br /><applet load="1grc" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1grc, resolution 3.0&Aring;" />
 
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'''CRYSTAL STRUCTURE OF GLYCINAMIDE RIBONUCLEOTIDE TRANSFORMYLASE FROM ESCHERICHIA COLI AT 3.0 ANGSTROMS RESOLUTION: A TARGET ENZYME FOR CHEMOTHERAPY'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF GLYCINAMIDE RIBONUCLEOTIDE TRANSFORMYLASE FROM ESCHERICHIA COLI AT 3.0 ANGSTROMS RESOLUTION: A TARGET ENZYME FOR CHEMOTHERAPY==
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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.
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<StructureSection load='1grc' size='340' side='right'caption='[[1grc]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1grc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GRC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GRC FirstGlance]. <br>
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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].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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==Reference==
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1grc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1grc OCA], [https://pdbe.org/1grc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1grc RCSB], [https://www.ebi.ac.uk/pdbsum/1grc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1grc ProSAT]</span></td></tr>
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Crystal structure of glycinamide ribonucleotide transformylase from Escherichia coli at 3.0 A resolution. A target enzyme for chemotherapy., Chen P, Schulze-Gahmen U, Stura EA, Inglese J, Johnson DL, Marolewski A, Benkovic SJ, Wilson IA, J Mol Biol. 1992 Sep 5;227(1):283-92. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1522592 1522592]
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PUR3_ECOLI PUR3_ECOLI]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gr/1grc_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1grc ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Phosphoribosylglycinamide formyltransferase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Chen P]]
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[[Category: Chen, P.]]
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[[Category: Wilson IA]]
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[[Category: Wilson, I.A.]]
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[[Category: PO4]]
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[[Category: transferase(formyl)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:14:52 2007''
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Current revision

CRYSTAL STRUCTURE OF GLYCINAMIDE RIBONUCLEOTIDE TRANSFORMYLASE FROM ESCHERICHIA COLI AT 3.0 ANGSTROMS RESOLUTION: A TARGET ENZYME FOR CHEMOTHERAPY

PDB ID 1grc

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