Open AccessCrystallization and preliminary X‐ray diffraction analysis of Bacillus subtilis YwfE, an l ‐amino‐acid ligase
Author(s) -
Tsuda Takeo,
Suzuki Tomomi,
Kojima Shuichi
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430911105425x
Subject(s) - bacillus subtilis , dipeptide , dna ligase , crystallization , amino acid , crystallography , crystal structure , substrate (aquarium) , chemistry , stereochemistry , bacteria , biochemistry , biology , enzyme , organic chemistry , ecology , genetics
Bacillus subtilis YwfE, an l ‐amino‐acid ligase, catalyzes the formation of an α‐dipeptide from l ‐amino acids in an ATP‐dependent manner. In order to elucidate the substrate‐recognition mode and the reaction mechanism of this ligase, native and selenomethionine‐derivatized (SeMet) crystals of YwfE in the presence of ADP, MgCl 2 and the dipeptide l ‐Ala‐ l ‐Gln were obtained using the hanging‐drop vapour‐diffusion method. These crystals diffracted to 1.9 and 2.8 Å resolution, respectively. Preliminary SAD phase calculations using the data set from the SeMet crystal suggested that the crystal belonged to the hexagonal space group P 6 5 22, with unit‐cell parameters a = b = 90.85, c = 250.31 Å, and contained one molecule in the asymmetric unit with a solvent content of 57.3%.