The Structure of l -Aspartate Ammonia-Lyase from Escherichia coli
| Autor: | Wuxian Shi, Maithri M. K. Jayasekera, Gregory K. Farber, Jennifer Dunbar, Ronald E. Viola |
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| Rok vydání: | 1997 |
| Předmět: |
Models
Molecular Protein Folding Stereochemistry Electrons Crystallography X-Ray Aspartate ammonia-lyase medicine.disease_cause Aspartate Ammonia-Lyase Biochemistry Catalysis Protein Structure Secondary Structure-Activity Relationship Tetramer Escherichia coli medicine chemistry.chemical_classification Binding Sites biology Chemistry Mutagenesis Substrate (chemistry) Active site Protein Structure Tertiary Enzyme Fumarase biology.protein Peptides |
| Zdroj: | Biochemistry. 36:9136-9144 |
| ISSN: | 1520-4995 0006-2960 |
| DOI: | 10.1021/bi9704515 |
| Popis: | The X-ray crystal structure of l-aspartate ammonia-lyase has been determined to 2.8 A resolution. The enzyme contains three domains, and each domain is composed almost completely of alpha helices. The central domain is composed of five long helices. In the tetramer, these five helices form a 20-helix cluster. Such clusters have also been seen in delta-crystallin and in fumarase. The active site of aspartase has been located in a region that contains side chains from three different subunits. The structure of the apoenzyme has made it possible to identify some of the residues that are involved in binding the substrate. These residues have been examined by site-directed mutagenesis, and their putative roles have been assigned [Jayasekera, M. M. K., Shi, W., Farber, G. K.,Viola, R. E. (1997) Biochemistry 36, 9145-9150]. |
| Databáze: | OpenAIRE |
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