Paper Report for: Rajakumara_2004_Acta.Crystallogr.D.Biol.Crystallogr_60_160
Reference
Title: Crystallization and preliminary X-ray crystallographic investigations on several thermostable forms of a Bacillus subtilis lipase Rajakumara E, Acharya P, Ahmad S, Shanmugam VM, Rao NM, Sankaranarayanan R Ref: Acta Crystallographica D Biol Crystallogr, 60:160, 2004 : PubMed
Bacillus subtilis lipase loses activity above pH 10.5 and below pH 6.0. However, at low pH, i.e. below pH 5.0, the lipase acquires remarkable thermostability. Activity was unaltered for 2 h at 323 K at pH 4.0-5.0, although at pH values above 7.0 the activity was lost rapidly within minutes. Circular-dichroism studies indicate significant changes in the tertiary structure of the lipase, whereas the secondary-structural content remained unaltered. To elucidate the structural basis of the enhanced thermostability, three different forms have been crystallized at low pH along with three crystal forms of two thermostable mutants obtained using a directed-evolution approach.
Rajakumara E, Acharya P, Ahmad S, Shanmugam VM, Rao NM, Sankaranarayanan R (2004) Crystallization and preliminary X-ray crystallographic investigations on several thermostable forms of a Bacillus subtilis lipase Acta Crystallographica D Biol Crystallogr60: 160-2
Rajakumara E, Acharya P, Ahmad S, Shanmugam VM, Rao NM, Sankaranarayanan R (2004) Acta Crystallographica D Biol Crystallogr60: 160-2