1TT9

Structure of the bifunctional and Golgi associated formiminotransferase cyclodeaminase octamer

Summary for 1TT9

• Entry DOI: 10.2210/pdb1tt9/pdb
• Descriptor: Formimidoyltransferase-cyclodeaminase (Formiminotransferase- cyclodeaminase) (FTCD) (58 kDa microtubule-binding protein) (1 entity in total)
• Functional Keywords: hepatitis autoantigen, intermediate channeling, protein assembly, vimentin, transferase, lyase
• Biological source: Rattus norvegicus (Norway rat)
• Cellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole : O88618
• Total number of polymer chains: 4
• Total formula weight: 237418.30

Authors

Mao, Y.,Vyas, N.K.,Vyas, M.N.,Chen, D.H.,Ludtke, S.J.,Chiu, W.,Quiocho, F.A. (deposition date: 2004-06-22, release date: 2005-06-28, Last modification date: 2024-02-14)

Primary citation

Mao, Y.,Vyas, N.K.,Vyas, M.N.,Chen, D.H.,Ludtke, S.J.,Chiu, W.,Quiocho, F.A.
Structure of the bifunctional and Golgi-associated formiminotransferase cyclodeaminase octamer
Embo J., 23:2963-2971, 2004

PubMed Abstract: 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.

PubMed: 15272307
DOI: 10.1038/sj.emboj.7600327

Experimental method

X-RAY DIFFRACTION (3.42 Å)