Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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].
The structure of L-aspartate ammonia-lyase from Escherichia coli.,Shi W, Dunbar J, Jayasekera MM, Viola RE, Farber GK Biochemistry. 1997 Jul 29;36(30):9136-44. PMID:9230045[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Shi W, Dunbar J, Jayasekera MM, Viola RE, Farber GK. The structure of L-aspartate ammonia-lyase from Escherichia coli. Biochemistry. 1997 Jul 29;36(30):9136-44. PMID:9230045 doi:10.1021/bi9704515
