|Protein Science (2007) 16(7):1360-7|
|Midwest Center for Structural Genomics|
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Crystal structures of two orthologs of the regulatory subunit of acetohydroxyacid synthase III (AHAS, EC 184.108.40.206) 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.
|metabolism enzymology chemistry genetics |
|Crystallography, X-Ray Models, Molecular Protein Structure, Tertiary Isoenzymes Molecular Sequence Data Arginine Thermotoga maritima Calcium Acetolactate Synthase Protein Structure, Secondary Amino Acid Sequence Protein Binding Sequence Homology, Amino Acid Bacterial Proteins |
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