The Structure of l-Aspartate Ammonia-Lyase from Escherichia coli,
- 1 July 1997
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 36 (30) , 9136-9144
- https://doi.org/10.1021/bi9704515
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].Keywords
This publication has 6 references indexed in Scilit:
- AMoRe: an automated package for molecular replacementActa Crystallographica Section A Foundations of Crystallography, 1994
- Aconitase, a two‐faced protein: enzyme and iron regulatory factor 1 2The FASEB Journal, 1993
- PROCHECK: a program to check the stereochemical quality of protein structuresJournal of Applied Crystallography, 1993
- MOLSCRIPT: a program to produce both detailed and schematic plots of protein structuresJournal of Applied Crystallography, 1991
- Kinetic studies of l-aspartase from Escherichia coli: pH-dependent activity changesArchives of Biochemistry and Biophysics, 1991
- The Temperature Dependence of the Steady State Kinetic Parameters of the Fumarase ReactionJournal of the American Chemical Society, 1963