1tt9
From Proteopedia
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Structure of the bifunctional and Golgi associated formiminotransferase cyclodeaminase octamer
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
1TT9 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 Nov 21 03:34:36 2007
