2FGC

Crystal structure of Acetolactate synthase- small subunit from Thermotoga maritima

Summary for 2FGC

• Entry DOI: 10.2210/pdb2fgc/pdb
• Descriptor: acetolactate synthase, small subunit, MAGNESIUM ION (3 entities in total)
• Functional Keywords: acetolactate synthase, regulatory subunit, structural genomics, psi, protein structure initiative, midwest center for structural genomics, mcsg, transferase
• Biological source: Thermotoga maritima
• Total number of polymer chains: 1
• Total formula weight: 22392.96

Authors

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) (deposition date: 2005-12-21, release date: 2006-02-07, Last modification date: 2022-04-13)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.3 Å)