2AT2

MOLECULAR STRUCTURE OF BACILLUS SUBTILIS ASPARTATE TRANSCARBAMOYLASE AT 3.0 ANGSTROMS RESOLUTION

2AT2 の概要

• エントリーDOI: 10.2210/pdb2at2/pdb
• 分子名称: ASPARTATE CARBAMOYLTRANSFERASE (1 entity in total)
• 機能のキーワード: transferase
• 由来する生物種: Bacillus subtilis
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 101325.39

構造登録者

Stevens, R.C.,Reinisch, K.M.,Lipscomb, W.N. (登録日: 1992-07-20, 公開日: 1994-01-31, 最終更新日: 2024-02-14)

主引用文献

Stevens, R.C.,Reinisch, K.M.,Lipscomb, W.N.
Molecular structure of Bacillus subtilis aspartate transcarbamoylase at 3.0 A resolution.
Proc.Natl.Acad.Sci.USA, 88:6087-6091, 1991

PubMed Abstract: The three-dimensional structure of Bacillus subtilis aspartate transcarbamoylase (ATCase; aspartate carbamoyltransferase; carbamoyl-phosphate:L-aspartate carbamoyltransferase, EC 2.1.3.2) has been solved by the molecular replacement method at 3.0 A resolution and refined to a crystallographic R factor of 0.19. The enzyme crystallizes in the space group C2 with unit cell dimensions a = 258.5, b = 153.2, and c = 51.9 A and beta = 97.7 degrees. The asymmetric unit is composed of three monomers related by noncrystallographic threefold symmetry. A total of 295 of 304 amino acid residues have been built into the monomer. The last 9 residues in the C terminus were not included in the final model. Each monomer consists of 34% alpha-helix and 18% beta-strand. Three solvent-exposed loop regions (residues 69-84, 178-191, and 212-229) are not well defined in terms of electron density. The catalytic trimer of ATCase from B. subtilis shows great similarity to the catalytic trimer in Escherichia coli ATCase, which was used in constructing the model for molecular replacement. The unliganded trimer from B. subtilis, which is not cooperative, resembles the T (inactive) state slightly more than the R (active)-state form of the E. coli trimer. However, certain regions in the B. subtilis trimer exhibit shifts toward the E. coli R-state conformation.

PubMed: 1906175
DOI: 10.1073/pnas.88.14.6087

実験手法

X-RAY DIFFRACTION (3 Å)