Open AccessCrystallization and preliminary X‐ray analysis of the rhamnogalacturonan lyase YesW from Bacillus subtilis strain 168, a member of polysaccharide lyase family 11
Author(s) -
Ochiai Akihito,
Yamasaki Masayuki,
Itoh Takafumi,
Mikami Bunzo,
Hashimoto Wataru,
Murata Kousaku
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106011894
Subject(s) - bacillus subtilis , crystallization , strain (injury) , lyase , chemistry , polysaccharide , biochemistry , crystallography , stereochemistry , microbiology and biotechnology , enzyme , biology , bacteria , organic chemistry , genetics , anatomy
Rhamnogalacturonan lyases degrade rhamnogalacturonan I, a major component of pectin, through a β‐elimination reaction. YesW from Bacillus subtilis strain 168 is a novel rhamnogalacturonan lyase classified into polysaccharide lyase family 11 (PL‐11). The enzyme was crystallized at 293 K using the sitting‐drop vapour‐diffusion method with 2‐methyl‐2,4‐pentanediol (MPD) as a precipitant. Preliminary X‐ray analysis revealed that the YesW crystals belong to space group P 2 1 and diffract to 2.40 Å resolution, with unit‐cell parameters a = 56.7, b = 105.6, c = 101.4 Å, β = 94.9°. This is the first report on the crystallization and preliminary X‐ray analysis of a family PL‐11 rhamnogalacturonan lyase.