X-ray analysis of two antibiotic-synthesizing bacterial ester hydrolases: preliminary results.
Alpha-amino-acid ester hydrolases are multimeric enzymes of potential use in antibiotic production. Knowledge of their structure could help to engineer these enzymes into economically viable biocatalysts. The alpha-amino-acid ester hydrolases from Xanthomonas citri and Acetobacter turbidans have been crystallized. The X. citri enzyme crystallizes in a primitive monoclinic space group (unit-cell parameters a = 90.1, b = 125.8, c = 132.1 A, beta = 90.9 degrees ). The A. turbidans enzyme crystallizes in both a primitive orthorhombic (a = 99.1, b = 104.9, c = 284.9 A) and a body-centred cubic space group with a = b = c = 342.2 A. From both enzymes, diffraction-quality crystals (resolution 3.0 A or better) were obtained. Data-collection statistics are reported for data sets from both enzymes.
Barends
Thomas R M
TR
Laboratory of Biophysical Chemistry, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands.
Hensgens
Charles M H
CM
Polderman-Tijmes
Jolanda J
JJ
Jekel
Peter A
PA
de Vries
Erik
E
Janssen
Dick B
DB
Dijkstra
Bauke W
BW
D000091:Acetobacter / Q000201:enzymology*; D000667:Ampicillin / Q000378:metabolism; D002265:Carboxylic Ester Hydrolases / Q000737:chemistry* / Q000378:metabolism; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods; D012984:Software; D014974:Xanthomonas / Q000201:enzymology*
D000667:Ampicillin; D002265:Carboxylic Ester Hydrolases; C058058:alpha-amino acid esterase