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2pfd

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[[Image:2pfd.gif|left|200px]]
 
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{{Structure
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==Anisotropically refined structure of FTCD==
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|PDB= 2pfd |SIZE=350|CAPTION= <scene name='initialview01'>2pfd</scene>, resolution 3.420&Aring;
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<StructureSection load='2pfd' size='340' side='right'caption='[[2pfd]], [[Resolution|resolution]] 3.42&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[2pfd]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PFD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PFD FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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|GENE= Ftcd ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1tt9|1tt9]]</div></td></tr>
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}}
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Ftcd ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>
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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=2pfd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pfd OCA], [https://pdbe.org/2pfd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pfd RCSB], [https://www.ebi.ac.uk/pdbsum/2pfd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pfd ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[https://www.uniprot.org/uniprot/FTCD_RAT FTCD_RAT]] Folate-dependent enzyme, that displays both transferase and deaminase activity. Serves to channel one-carbon units from formiminoglutamate to the folate pool (By similarity).<ref>PMID:12160147</ref> Binds and promotes bundling of vimentin filaments originating from the Golgi.<ref>PMID:12160147</ref>
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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/pf/2pfd_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=2pfd 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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Mammalian formiminotransferase cyclodeaminase (FTCD), a 0.5 million Dalton homo-octameric enzyme, plays important roles in coupling histidine catabolism with folate metabolism and integrating the Golgi complex with the vimentin intermediate filament cytoskeleton. It is also linked to two human diseases, autoimmune hepatitis and glutamate formiminotransferase deficiency. Determination of the FTCD structure by X-ray crystallography and electron cryomicroscopy revealed that the eight subunits, each composed of distinct FT and CD domains, are arranged like a square doughnut. A key finding indicates that coupling of three subunits governs the octamer-dependent sequential enzyme activities, including channeling of intermediate and conformational change. The structure further shed light on the molecular nature of two strong antigenic determinants of FTCD recognized by autoantibodies from patients with autoimmune hepatitis and on the binding of thin vimentin filaments to the FTCD octamer.
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'''Anisotropically refined structure of FTCD'''
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Structure of the bifunctional and Golgi-associated formiminotransferase cyclodeaminase octamer.,Mao Y, Vyas NK, Vyas MN, Chen DH, Ludtke SJ, Chiu W, Quiocho FA EMBO J. 2004 Aug 4;23(15):2963-71. Epub 2004 Jul 22. PMID:15272307<ref>PMID:15272307</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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==About this Structure==
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</div>
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2PFD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PFD OCA].
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<div class="pdbe-citations 2pfd" style="background-color:#fffaf0;"></div>
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[[Category: Rattus norvegicus]]
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== References ==
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[[Category: Single protein]]
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<references/>
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[[Category: Chen, X.]]
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__TOC__
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[[Category: Lu, M.]]
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</StructureSection>
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[[Category: Ma, J.]]
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[[Category: Buffalo rat]]
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[[Category: Poon, B K.]]
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[[Category: Large Structures]]
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[[Category: Quiocho, F A.]]
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[[Category: Chen, X]]
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[[Category: Wang, Q.]]
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[[Category: Lu, M]]
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[[Category: protein assembly]]
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[[Category: Ma, J]]
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[[Category: Poon, B K]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:12:15 2008''
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[[Category: Quiocho, F A]]
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[[Category: Wang, Q]]
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[[Category: Lyase]]
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[[Category: Protein assembly]]
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[[Category: Transferase]]

Current revision

Anisotropically refined structure of FTCD

PDB ID 2pfd

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