1TT9

Structure of the bifunctional and Golgi associated formiminotransferase cyclodeaminase octamer

1TT9 の概要

• エントリーDOI: 10.2210/pdb1tt9/pdb
• 分子名称: Formimidoyltransferase-cyclodeaminase (Formiminotransferase- cyclodeaminase) (FTCD) (58 kDa microtubule-binding protein) (1 entity in total)
• 機能のキーワード: hepatitis autoantigen, intermediate channeling, protein assembly, vimentin, transferase, lyase
• 由来する生物種: Rattus norvegicus (Norway rat)
• 細胞内の位置: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole : O88618
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 237418.30

構造登録者

Mao, Y.,Vyas, N.K.,Vyas, M.N.,Chen, D.H.,Ludtke, S.J.,Chiu, W.,Quiocho, F.A. (登録日: 2004-06-22, 公開日: 2005-06-28, 最終更新日: 2024-02-14)

主引用文献

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

実験手法

X-RAY DIFFRACTION (3.42 Å)