Crystallization and preliminary X-ray analysis of Aes, an acetyl-esterase from Escherichia coli.
Aes belongs to the family of hormone-sensitive lipases and has acetyl-esterase activity. It is also known to control maltose uptake through interaction with MalT, the central regulator of the Escherichia coli maltose system. Aes was crystallized as an N-terminally His(6)-tagged protein both in the native form and with selenomethionine substitution. Crystals grew in both cases in space group R32 to dimensions of about 0.2 x 0.15 x 0.05 mm (native His(6)-Aes) and about 0.5 x 0.3 x 0.1 mm (SeMet-His(6)-Aes). A native data set has been obtained at 2.4 A resolution; the selenomethionine-substituted Aes crystals diffracted to 3.0 A resolution.
Department of Biology, University of Konstanz, D-78457 Konstanz, Germany. kinga44@yahoo.com
Kinga
K
Gerber
André
A
Schiefner
Peter
P
Seige
Kay
K
Diederichs
Winfried
W
Boos
Wolfram
W
Welte
D000115:Acetylesterase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D003460:Crystallization; D018360:Crystallography, X-Ray; D004268:DNA-Binding Proteins / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D011485:Protein Binding; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D014157:Transcription Factors / Q000378:metabolism*
D004268:DNA-Binding Proteins; D029968:Escherichia coli Proteins; C058976:MalT protein, E coli; D011993:Recombinant Fusion Proteins; D014157:Transcription Factors; D000115:Acetylesterase