1zly

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{{Seed}}
 
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[[Image:1zly.png|left|200px]]
 
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==The structure of human glycinamide ribonucleotide transformylase in complex with alpha,beta-N-(hydroxyacetyl)-D-ribofuranosylamine and 10-formyl-5,8,dideazafolate==
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The line below this paragraph, containing "STRUCTURE_1zly", creates the "Structure Box" on the page.
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<StructureSection load='1zly' size='340' side='right'caption='[[1zly]], [[Resolution|resolution]] 2.07&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1zly]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZLY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZLY FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2.07&#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=DQB:4-[(4-{[(2-AMINO-4-OXO-3,4-DIHYDROQUINAZOLIN-6-YL)METHYL]AMINO}BENZOYL)AMINO]BUTANOIC+ACID'>DQB</scene>, <scene name='pdbligand=GRF:5-O-PHOSPHONO-BETA-D-RIBOFURANOSYLAMINE'>GRF</scene></td></tr>
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{{STRUCTURE_1zly| PDB=1zly | SCENE= }}
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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=1zly FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zly OCA], [https://pdbe.org/1zly PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zly RCSB], [https://www.ebi.ac.uk/pdbsum/1zly PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zly ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PUR2_HUMAN PUR2_HUMAN]
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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/zl/1zly_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=1zly ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Glycinamide ribonucleotide transformylase (GART; 10-formyltetrahydrofolate:5'-phosphoribosylglycinamide formyltransferase, EC 2.1.2.2), an essential enzyme in de novo purine biosynthesis, has been a chemotherapeutic target for several decades. The three-dimensional structure of the GART domain from the human trifunctional enzyme has been solved by X-ray crystallography. Models of the apoenzyme, and a ternary complex with the 10-formyl-5,8-dideazafolate cosubstrate and a glycinamide ribonucleotide analogue, hydroxyacetamide ribonucleotide [alpha,beta-N-(hydroxyacetyl)-d-ribofuranosylamine], are reported to 2.2 and 2.07 A, respectively. The model of the apoenzyme represents the first structure of GART, from any source, with a completely unoccupied substrate and cosubstrate site, while the ternary complex is the first structure of the human GART domain that is bound at both the substrate and cosubstrate sites. A comparison of the two models therefore reveals subtle structural differences that reflect substrate and cosubstrate binding effects and implies roles for the invariant residues Gly 133, Gly 146, and His 137. Preactivation of the DDF formyl group appears to be key for catalysis, and structural flexibility of the active end of the substrate may facilitate nucleophilic attack. A change in pH, rather than folate binding, correlates with movement of the folate binding loop, whereas the phosphate binding loop position does not vary with pH. The electrostatic surface potentials of the human GART domain and Escherichia coli enzyme explain differences in the binding affinity of polyglutamylated folates, and these differences have implications to future chemotherapeutic agent design.
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===The structure of human glycinamide ribonucleotide transformylase in complex with alpha,beta-N-(hydroxyacetyl)-D-ribofuranosylamine and 10-formyl-5,8,dideazafolate===
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The apo and ternary complex structures of a chemotherapeutic target: human glycinamide ribonucleotide transformylase.,Dahms TE, Sainz G, Giroux EL, Caperelli CA, Smith JL Biochemistry. 2005 Jul 26;44(29):9841-50. PMID:16026156<ref>PMID:16026156</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_16026156}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1zly" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 16026156 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_16026156}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1ZLY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZLY OCA].
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==Reference==
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The apo and ternary complex structures of a chemotherapeutic target: human glycinamide ribonucleotide transformylase., Dahms TE, Sainz G, Giroux EL, Caperelli CA, Smith JL, Biochemistry. 2005 Jul 26;44(29):9841-50. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16026156 16026156]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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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: Caperelli CA]]
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[[Category: Caperelli, C A.]]
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[[Category: Dahms TES]]
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[[Category: Dahms, T E.S.]]
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[[Category: Giroux EL]]
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[[Category: Giroux, E L.]]
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[[Category: Sainz G]]
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[[Category: Sainz, G.]]
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[[Category: Smith JL]]
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[[Category: Smith, J L.]]
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[[Category: Purine biosynthesis]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 05:01:10 2008''
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Current revision

The structure of human glycinamide ribonucleotide transformylase in complex with alpha,beta-N-(hydroxyacetyl)-D-ribofuranosylamine and 10-formyl-5,8,dideazafolate

PDB ID 1zly

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