1DBF

CHORISMATE MUTASE FROM BACILLUS SUBTILIS AT 1.30 ANGSTROM

1DBF の概要

• エントリーDOI: 10.2210/pdb1dbf/pdb
• 分子名称: PROTEIN (CHORISMATE MUTASE), SULFATE ION, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: chorismate mutase, shikimate pathway, isomerase
• 由来する生物種: Bacillus subtilis
• 細胞内の位置: Cytoplasm : P19080
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 44848.78

構造登録者

Gilliland, G.L.,Ladner, J.E. (登録日: 1999-11-02, 公開日: 2000-06-07, 最終更新日: 2023-08-09)

主引用文献

Ladner, J.E.,Reddy, P.,Davis, A.,Tordova, M.,Howard, A.J.,Gilliland, G.L.
The 1.30 A resolution structure of the Bacillus subtilis chorismate mutase catalytic homotrimer.
Acta Crystallogr.,Sect.D, 56:673-683, 2000

PubMed Abstract: 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.

PubMed: 10818343
DOI: 10.1107/S0907444900004625

実験手法

X-RAY DIFFRACTION (1.3 Å)