Detection of α/β-hydrolase fold in the cell surface esterases of Acinetobacter species using an analysis of 3D profiles

Rinat N. Alon, Leonid Mirny, Joel L. Sussman, David L. Gutnick

Research output: Contribution to journalArticlepeer-review

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 α/β proteins and specifically to those with the α/β-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.

Original languageEnglish
Pages (from-to)231-235
Number of pages5
JournalFEBS Letters
Volume371
Issue number3
DOIs
StatePublished - 11 Sep 1995

Keywords

  • Acinetobacter
  • Esterase
  • Structural alignment
  • α/β Hydrolase fold

Fingerprint

Dive into the research topics of 'Detection of α/β-hydrolase fold in the cell surface esterases of Acinetobacter species using an analysis of 3D profiles'. Together they form a unique fingerprint.

Cite this