2pc6

Crystal structure of putative acetolactate synthase- small subunit from Nitrosomonas europaea

spinqualitylabelsall models 2pc6, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2pc6 is a 4 chain structure with sequence from Niteu. This structure supersedes the now removed PDB entry 2fgd. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, UNL NonStd Res: MSE Related: 2fgd, 2fgc Gene: ilvH, NE1324 (NITEU) Activity: Lyase, with EC number 4.1.3.18 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Crystal structures of TM0549 and NE1324--two orthologs of E. coli AHAS isozyme III small regulatory subunit.,Petkowski JJ, Chruszcz M, Zimmerman MD, Zheng H, Skarina T, Onopriyenko O, Cymborowski MT, Koclega KD, Savchenko A, Edwards A, Minor W Protein Sci. 2007 Jul;16(7):1360-7. PMID:17586771 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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