Crystallization and rhenium MAD phasing of the acyl-homoserinelactone synthase EsaI

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 synth...

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Bibliographic Details
Published in:Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2009-04, Vol.57 (2001)
Main Authors: Watson, W.T., Murphy IV, Frank V., Gould, Ty A., Jambeck, Per, Val, Dale L., Cronan, Jr., John E., Beck von Bodman, Susan, Churchill, Mair E.A.
Format: Article
Language:English
Subjects:
BACTERIA
BASIC BIOLOGICAL SCIENCES
BIOLOGICAL FUNCTIONS
CRYSTAL STRUCTURE
CRYSTALLIZATION
GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE
LACTONES
PERRHENATES
RHENIUM
SPACE GROUPS
VIRULENCE
X-RAY DIFFRACTION
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Summary: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{sub 3}, with unit-cell parameters a = b = 66.40, c = 47.33 {angstrom}. 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 {angstrom} and the perrhenate ion binding sites and liganding residues have been identified.
ISSN:0907-4449
1399-0047