Crystallization and preliminary X-ray crystallographic studies of enoyl-acyl carrier protein reductase (FabI) from Psuedomonas aeruginosa

Jeong Hye Lee, Ae Kyung Park, Young Min Chi, Jin Ho Moon, Ki Seog Lee

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

During fatty-acid biosynthesis, enoyl-acyl carrier protein (enoyl-ACP) reductase catalyzes the reduction of trans-2-enoyl-ACP to fully saturated acyl-ACP via the ubiquitous fatty-acid synthase system. NADH-dependent enoyl-ACP reductase (FabI) from Pseudomonas aeruginosa has been purified and crystallized as an apoenzyme and in a complex form with NADH and triclosan. Triclosan is an inhibitor of FabI and forms a stable ternary complex in the presence of NADH. The crystals of native and complexed FabI diffracted to resolutions of 2.6 and 1.8 Å, respectively. The crystals both belonged to space group P21, with unit-cell parameters a = 117.32, b = 155.844, c = 129.448 Å, Β = 111.061° for the native enzyme and a = 64.784, b = 107.573, c = 73.517 Å, Β = 116.162° for the complex. Preliminary molecular replacement further confirmed the presence of four tetramers of native FabI and one tetramer of the complex in the asymmetric unit, corresponding to Matthews coefficients (V M) of 2.46 and 2.05 Å 3 Da -1 and solvent contents of 50.1 and 40.1%, respectively.

Original languageEnglish
Pages (from-to)214-216
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume67
Issue number2
DOIs
Publication statusPublished - 2011 Feb 1

Keywords

  • Enoyl-acyl carrier protein reductases
  • FabI
  • Fatty-acid synthesis
  • Pseudomonas aeruginosa
  • Triclosan

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Structural Biology
  • Genetics
  • Condensed Matter Physics

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