2pfd

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'''Anisotropically refined structure of FTCD'''
'''Anisotropically refined structure of FTCD'''
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==Overview==
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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.
==About this Structure==
==About this Structure==
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].
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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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15272307 15272307]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Quiocho, F A.]]
[[Category: Quiocho, F A.]]
[[Category: Wang, Q.]]
[[Category: Wang, Q.]]
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[[Category: Lyase]]
[[Category: Protein assembly]]
[[Category: Protein assembly]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 13:00:03 2008''
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 14 11:38:51 2008''

Revision as of 08:38, 14 May 2008

Template:STRUCTURE 2pfd

Anisotropically refined structure of FTCD


Overview

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.

About this Structure

2PFD is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Wed May 14 11:38:51 2008

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