2pfd

From Proteopedia

(Difference between revisions)

Revision as of 15:22, 17 June 2021

Anisotropically refined structure of FTCD

Structural highlights

2pfd is a 4 chain structure with sequence from Buffalo rat. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Related:	1tt9
Gene:	Ftcd (Buffalo rat)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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).^[1] Binds and promotes bundling of vimentin filaments originating from the Golgi.^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Gao YS, Vrielink A, MacKenzie R, Sztul E. A novel type of regulation of the vimentin intermediate filament cytoskeleton by a Golgi protein. Eur J Cell Biol. 2002 Jul;81(7):391-401. PMID:12160147 doi:10.1078/0171-9335-00260
↑ Gao YS, Vrielink A, MacKenzie R, Sztul E. A novel type of regulation of the vimentin intermediate filament cytoskeleton by a Golgi protein. Eur J Cell Biol. 2002 Jul;81(7):391-401. PMID:12160147 doi:10.1078/0171-9335-00260
↑ Mao Y, Vyas NK, Vyas MN, Chen DH, Ludtke SJ, Chiu W, Quiocho FA. Structure of the bifunctional and Golgi-associated formiminotransferase cyclodeaminase octamer. EMBO J. 2004 Aug 4;23(15):2963-71. Epub 2004 Jul 22. PMID:15272307 doi:10.1038/sj.emboj.7600327

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2pfd"

@@ Line 1: / Line 1: @@
 ==Anisotropically refined structure of FTCD==
-<StructureSection load='2pfd' size='340' side='right' caption='[[2pfd]], [[Resolution|resolution]] 3.42&Aring;' scene=''>
+<StructureSection load='2pfd' size='340' side='right'caption='[[2pfd]], [[Resolution|resolution]] 3.42&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2pfd]] is a 4 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2PFD FirstGlance]. <br>
+<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>
 </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>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1tt9|1tt9]]</td></tr>
+<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>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Ftcd ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>
+<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>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2pfd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pfd OCA], [http://pdbe.org/2pfd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2pfd RCSB], [http://www.ebi.ac.uk/pdbsum/2pfd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2pfd ProSAT]</span></td></tr>
+<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>
 </table>
 == Function ==
-[[http://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>
+[[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>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 35: / Line 35: @@
 </StructureSection>
 [[Category: Buffalo rat]]
+[[Category: Large Structures]]
 [[Category: Chen, X]]
 [[Category: Lu, M]]

2pfd

From Proteopedia

Revision as of 15:22, 17 June 2021

Anisotropically refined structure of FTCD

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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