1qd1

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(New page: 200px<br /><applet load="1qd1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qd1, resolution 1.7&Aring;" /> '''THE CRYSTAL STRUCTURE...)
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[[Image:1qd1.jpg|left|200px]]<br /><applet load="1qd1" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1qd1, resolution 1.7&Aring;" />
 
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'''THE CRYSTAL STRUCTURE OF THE FORMIMINOTRANSFERASE DOMAIN OF FORMIMINOTRANSFERASE-CYCLODEAMINASE.'''<br />
 
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==Overview==
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==THE CRYSTAL STRUCTURE OF THE FORMIMINOTRANSFERASE DOMAIN OF FORMIMINOTRANSFERASE-CYCLODEAMINASE.==
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BACKGROUND: The bifunctional enzyme formiminotransferase-cyclodeaminase, (FTCD) contains two active sites at different positions on the protein, structure. The enzyme binds a gamma-linked polyglutamylated form of the, tetrahydrofolate substrate and channels the product of the transferase, reaction from the transferase active site to the cyclodeaminase active, site. Structural studies of this bifunctional enzyme and its, monofunctional domains will provide insight into the mechanism of, substrate channeling and the two catalytic reactions. RESULTS: The crystal, structure of the formiminotransferase (FT) domain of FTCD has been, determined in the presence of a product analog, folinic acid. The overall, structure shows that the FT domain comprises two subdomains that adopt a, novel alpha/beta fold. Inspection of the folinic acid binding site reveals, an electrostatic tunnel traversing the width of the molecule. The, distribution of charged residues in the tunnel provides insight into the, possible mode of substrate binding and channeling. The electron density, reveals that the non-natural stereoisomer, (6R)-folinic acid, binds to the, protein; this observation suggests a mechanism for product release. In, addition, a single molecule of glycerol is bound to the enzyme and, indicates a putative binding site for formiminoglutamate. CONCLUSIONS: The, structure of the FT domain in the presence of folinic acid reveals a, possible novel mechanism for substrate channeling. The position of the, folinic acid and a bound glycerol molecule near to the sidechain of His82, suggests that this residue may act as the catalytic base required for the, formiminotransferase mechanism.
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<StructureSection load='1qd1' size='340' side='right'caption='[[1qd1]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1qd1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QD1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QD1 FirstGlance]. <br>
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1QD1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with FON and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Glutamate_formimidoyltransferase Glutamate formimidoyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.2.5 2.1.2.5] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QD1 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]] 1.7&#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=FON:N-{[4-({[(6R)-2-AMINO-5-FORMYL-4-OXO-1,4,5,6,7,8-HEXAHYDROPTERIDIN-6-YL]METHYL}AMINO)PHENYL]CARBONYL}-L-GLUTAMIC+ACID'>FON</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=1qd1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qd1 OCA], [https://pdbe.org/1qd1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qd1 RCSB], [https://www.ebi.ac.uk/pdbsum/1qd1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qd1 ProSAT]</span></td></tr>
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The crystal structure of the formiminotransferase domain of formiminotransferase-cyclodeaminase: implications for substrate channeling in a bifunctional enzyme., Kohls D, Sulea T, Purisima EO, MacKenzie RE, Vrielink A, Structure. 2000 Jan 15;8(1):35-46. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10673422 10673422]
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</table>
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[[Category: Glutamate formimidoyltransferase]]
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== Function ==
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[[Category: Single protein]]
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[https://www.uniprot.org/uniprot/FTCD_PIG FTCD_PIG] Folate-dependent enzyme, that displays both transferase and deaminase activity. Serves to channel one-carbon units from formiminoglutamate to the folate pool. Binds and promotes bundling of vimentin filaments originating from the Golgi (By similarity).
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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/qd/1qd1_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=1qd1 ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
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[[Category: Kohls, D.]]
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[[Category: Kohls D]]
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[[Category: MacKenzie, R.E.]]
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[[Category: MacKenzie RE]]
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[[Category: Purisima, E.]]
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[[Category: Purisima E]]
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[[Category: Sulea, T.]]
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[[Category: Sulea T]]
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[[Category: Vrielink, A.]]
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[[Category: Vrielink A]]
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[[Category: FON]]
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[[Category: GOL]]
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[[Category: alpha-beta-beta-alpha sandwich]]
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[[Category: electrostatically charged substrate tunnel]]
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[[Category: functional dimer]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:35:15 2007''
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Current revision

THE CRYSTAL STRUCTURE OF THE FORMIMINOTRANSFERASE DOMAIN OF FORMIMINOTRANSFERASE-CYCLODEAMINASE.

PDB ID 1qd1

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