PMID:9230045

Citation	Shi, W, Dunbar, J, Jayasekera, MM, Viola, RE and Farber, GK (1997) The structure of L-aspartate ammonia-lyase from Escherichia coli. Biochemistry 36:9136-44
Abstract	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].
Links	PubMed Online version:10.1021/bi9704515
Keywords	Aspartate Ammonia-Lyase/chemistry; Binding Sites; Catalysis; Crystallography, X-Ray; Electrons; Escherichia coli/chemistry; Escherichia coli/enzymology; Models, Molecular; Peptides/chemistry; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; Structure-Activity Relationship
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