2FGC

Crystal structure of Acetolactate synthase- small subunit from Thermotoga maritima

2FGC の概要

• エントリーDOI: 10.2210/pdb2fgc/pdb
• 分子名称: acetolactate synthase, small subunit, MAGNESIUM ION (3 entities in total)
• 機能のキーワード: acetolactate synthase, regulatory subunit, structural genomics, psi, protein structure initiative, midwest center for structural genomics, mcsg, transferase
• 由来する生物種: Thermotoga maritima
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 22392.96

構造登録者

Petkowski, J.J.,Chruszcz, M.,Zimmerman, M.D.,Zheng, H.,Cymborowski, M.T.,Koclega, K.D.,Kudritska, M.,Minor, W.,Midwest Center for Structural Genomics (MCSG) (登録日: 2005-12-21, 公開日: 2006-02-07, 最終更新日: 2024-11-06)

主引用文献

Petkowski, J.J.,Chruszcz, M.,Zimmerman, M.D.,Zheng, H.,Skarina, T.,Onopriyenko, O.,Cymborowski, M.T.,Koclega, K.D.,Savchenko, A.,Edwards, A.,Minor, W.
Crystal structures of TM0549 and NE1324--two orthologs of E. coli AHAS isozyme III small regulatory subunit.
Protein Sci., 16:1360-1367, 2007

PubMed Abstract: Crystal structures of two orthologs of the regulatory subunit of acetohydroxyacid synthase III (AHAS, EC 2.2.1.6) from Thermotoga maritima (TM0549) and Nitrosomonas europea (NE1324) were determined by single-wavelength anomalous diffraction methods with the use of selenomethionine derivatives at 2.3 A and 2.5 A, respectively. TM0549 and NE1324 share the same fold, and in both proteins the polypeptide chain contains two separate domains of a similar size. Each protein contains a C-terminal domain with ferredoxin-type fold and an N-terminal ACT domain, of which the latter is characteristic for several proteins involved in amino acid metabolism. The ferredoxin domain is stabilized by a calcium ion in the crystal structure of NE1324 and by a Mg(H2O)(6)2+ ion in TM0549. Both TM0549 and NE1324 form dimeric assemblies in the crystal lattice.

PubMed: 17586771
DOI: 10.1110/ps.072793807

実験手法

X-RAY DIFFRACTION (2.3 Å)