Crystallization and Rhenium MAD Phasing of the Acyl-Homoserinelactone Synthase EsaI

Acta Crystallogr D Biol Crystallogr. 2001 Dec;57(Pt 12):1945-9. doi: 10.1107/s0907444901014512. Epub 2001 Nov 21.

Abstract

Acyl-homoserine-L-lactones (AHLs) are diffusible chemical signals that are required for virulence of many Gram-negative bacteria. AHLs are produced by AHL synthases from two substrates, S-adenosyl-L-methionine and acyl-acyl carrier protein. The AHL synthase EsaI, which is homologous to the AHL synthases from other pathogenic bacterial species, has been crystallized in the primitive tetragonal space group P4(3), with unit-cell parameters a = b = 66.40, c = 47.33 A. The structure was solved by multiple-wavelength anomalous diffraction with a novel use of the rhenium anomalous signal. The rhenium-containing structure has been refined to a resolution of 2.5 A and the perrhenate ion binding sites and liganding residues have been identified.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Bacterial Proteins / chemistry*
  • Crystallization
  • Crystallography, X-Ray
  • Models, Molecular
  • Pantoea / enzymology*
  • Protein Conformation
  • Rhenium / chemistry*

Substances

  • Bacterial Proteins
  • EsaI protein, Erwinia stewartii
  • Rhenium

Associated data

  • PDB/1K4J