Abstract

Article info 2017 5 (1)    005  (01)   pp.  40 ~ 43
Title Crystallization and preliminary crystallographic analysis of IlvC, a ketol-acid reductoisomerase, from Streptococcus pneumoniae
Authors Gyuhee Kim and Sangho Lee*
Institutions Department of Biological Sciences, Sungkyunkwan University, 2066 Seobu-ro, Suwon, Gyeonggi 16419, Korea. *Correspondence: sangholee@skku.edu
Abstract IlvC, a ketol-acid reductoisomerase, plays a critical role in alkyl migration and catalyzes the second step in the biosynthesis of branched amino acids such as leucine, valine and isoleucine. As an initial step to investigate whether IlvC is involved in pneumococcal growth and virulence from the structural background, ilvC from Streptococcus pneumoniae D39 (SpIlvC) was cloned and overexpressed in Escherichia coli. Crystals of SpIlvC were obtained by hanging-drop vapour diffusion in 0.1 M HEPES pH 7.5, 0.1 M NaCl, 1.5 M ammonium sulfate and diffracted to 1.69 Å resolution. The SpIlvC crystal belonged to space group P2 1 2 1 2 1 with unit cell parameters a = 69.1°, b = 104.3°, c = 110.9° and contained two molecules in the asymmetric unit.