1CSM

THE CRYSTAL STRUCTURE OF ALLOSTERIC CHORISMATE MUTASE AT 2.2 ANGSTROMS RESOLUTION

Summary for 1CSM

• Entry DOI: 10.2210/pdb1csm/pdb
• Descriptor: CHORISMATE MUTASE, TRYPTOPHAN (3 entities in total)
• Functional Keywords: isomerase
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Total number of polymer chains: 2
• Total formula weight: 60010.90

Authors

Xue, Y.,Lipscomb, W.N. (deposition date: 1994-08-22, release date: 1995-09-15, Last modification date: 2024-02-07)

Primary citation

Xue, Y.,Lipscomb, W.N.,Graf, R.,Schnappauf, G.,Braus, G.
The crystal structure of allosteric chorismate mutase at 2.2-A resolution.
Proc.Natl.Acad.Sci.USA, 91:10814-10818, 1994

PubMed Abstract: The crystal structure of an allosteric chorismate mutase, the Thr-226-->Ile mutant, from yeast Saccharomyces cerevisiae has been determined to 2.2-A resolution by using the multiple isomorphous replacement method. Solvent-flattening and electron-density modification were applied for phase improvement. The current crystallographic R factor is 0.196. The final model includes 504 of the 512 residues and 97 water molecules. In addition, two tryptophan molecules were identified in the interface between monomers. The overall structure is completely different from the reported structure of chorismate mutase from Bacillus subtilis. This structure showed 71% helices with essentially no beta-sheet structures.

PubMed: 7971967
DOI: 10.1073/pnas.91.23.10814

Experimental method

X-RAY DIFFRACTION (2.2 Å)