Detection of alpha/beta-hydrolase fold in the cell surface esterases of Acinetobacter species using an analysis of 3D profiles.
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.
Alon
R N
RN
Department of Molecular Microbiology and Biotechnology, George S. Wise Faculty of Life Sciences, Tel Aviv University, Ramat-Aviv, Israel.
Mirny
L
L
Sussman
J L
JL
Gutnick
D L
DL
D000150:Acinetobacter / Q000201:enzymology*; D016954:Acinetobacter calcoaceticus / Q000737:chemistry*; D000465:Algorithms; D000595:Amino Acid Sequence; D000818:Animals; D001426:Bacterial Proteins / Q000737:chemistry*; D004950:Esterases / Q000737:chemistry*; D006801:Humans; D006867:Hydrolases / Q000737:chemistry*; D008565:Membrane Proteins / Q000737:chemistry; D008969:Molecular Sequence Data; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid
D001426:Bacterial Proteins; D008565:Membrane Proteins; D006867:Hydrolases; D004950:Esterases