NDLI: Molecular structure of Bacillus subtilis aspartate transcarbamoylase at 3.0 A resolution.

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Molecular structure of Bacillus subtilis aspartate transcarbamoylase at 3.0 A resolution.

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Two-dimensional life?

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Molecular structure of Bacillus subtilis aspartate transcarbamoylase at 3.0 A resolution.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Reinisch, K. M. Stevens, R. C. Lipscomb, W. N.
Description	Author Affiliation: Stevens RC ( Gibbs Chemical Laboratory, Harvard University, Cambridge, MA 02138.);
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.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	14
Volume Number	88
Language	English
Publisher	National Academy of Sciences
Publisher Date	1991-08-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Aspartate Carbamoyltransferase Chemistry Bacillus Subtilis Enzymology Amino Acid Sequence Genetics Isolation & Purification Escherichia Coli Macromolecular Substances Models, Molecular Molecular Sequence Data Protein Conformation Sequence Homology, Nucleic Acid X-Ray Diffraction Comparative Study Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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