The crystal structure of allosteric chorismate mutase at 2.2-A resolution.
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.
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Gibbs Chemical Laboratory, Harvard University, Cambridge, MA 02138.
Lipscomb
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Graf
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Schnappauf
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Braus
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D000494:Allosteric Regulation; D001665:Binding Sites; D002826:Chorismate Mutase / Q000737:chemistry*; D018360:Crystallography, X-Ray; D005656:Fungal Proteins / Q000737:chemistry; D006860:Hydrogen Bonding; D008958:Models, Molecular; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D012995:Solubility; D014364:Tryptophan / Q000737:chemistry
D005656:Fungal Proteins; D014364:Tryptophan; D002826:Chorismate Mutase