1dbf
From Proteopedia
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CHORISMATE MUTASE FROM BACILLUS SUBTILIS AT 1.30 ANGSTROM
Overview
The crystal structure of the Bacillus subtilis chorismate mutase, an, enzyme of the aromatic amino acids biosynthetic pathway, was determined to, 1.30 A resolution. The structure of the homotrimer was determined by, molecular replacement using orthorhombic crystals of space group, P2(1)2(1)2(1) with unit-cell parameters a = 52.2, b = 83. 8, c = 86.0 A., The ABC trimer of the monoclinic crystal structure [Chook et al. (1994), J. Mol. Biol. 240, 476-500] was used as the starting model. The final, coordinates are composed of three complete polypeptide chains of 127, amino-acid residues. In addition, there are nine sulfate ions, five, glycerol molecules and 424 water molecules clearly visible in the, structure. This structure was refined with aniosotropic temperature, factors, has excellent geometry and a crystallographic R factor of 0.169, with an R(free) of 0.236. The three active sites of the macromolecule are, at the subunit interfaces, with residues from two subunits contributing to, each site. This orthorhombic crystal form was grown using ammonium sulfate, as the precipitant; glycerol was used as a cryoprotectant during data, collection. A glycerol molecule and sulfate ion in each of the active, sites was found mimicking a transition-state analog. In this structure, the C-terminal tails of the subunits of the trimer are hydrogen bonded to, residues of the active site of neighboring trimers in the crystal and thus, cross-link the molecules in the crystal lattice.
About this Structure
1DBF is a Single protein structure of sequence from Bacillus subtilis with SO4 and GOL as ligands. Active as Chorismate mutase, with EC number 5.4.99.5 Full crystallographic information is available from OCA.
Reference
The 1.30 A resolution structure of the Bacillus subtilis chorismate mutase catalytic homotrimer., Ladner JE, Reddy P, Davis A, Tordova M, Howard AJ, Gilliland GL, Acta Crystallogr D Biol Crystallogr. 2000 Jun;56(Pt 6):673-83. PMID:10818343
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