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Detection of alpha/beta-hydrolase fold in the cell surface esterases of Acinetobacter species using an analysis of 3D
R N Alon1, L Mirny, J L Sussman
1Department of Molecular Microbiology and Biotechnology, George S. Wise Faculty of Life Sciences, Tel Aviv University, Ramat-Aviv, Israel.
FEBS Letters
|September 11, 1995
Abstract:
The primary sequence of esterases from Acinetobacter lwoffii RAG-1 and A. calcoaceticus BD413 were compared with linearized structural sequences of two hundred proteins selected from Brookhaven Protein DataBank using a modified version of the Bowie et al. algorithm [3]. Significant structural homology was found to alpha/beta proteins and specifically to those with the alpha/beta-hydrolase fold for which the crystal structure was reported. No such homology was detected using common primary sequence alignment programs such as FASTA or BLAST.