Research article - Peer-reviewed, 2004
X-ray structure of peptidyl-prolyl cis-trans isomerase A from Mycobacterium tuberculosis
Henriksson LM, Johansson P, Unge T, Mowbray SLAbstract
Peptidyl-prolyl cis-trans isomerases (EC 5.2.1.8) catalyse the interconversion of cis and trans peptide bonds and are therefore considered to be important for protein folding. They are also thought to participate in processes such as signalling, cell surface recognition, chaperoning and heat-shock response. Here we report the soluble expression of recombinant Mycobacterium tuberculosis peptidyl-prolyl cis-trans isomerase PpiA in Escherichia coli, together with an investigation of its structure and biochemical properties. The protein was shown to be active in a spectrophotometric assay, with an estimated k(cat)/K-m of 2.0 x 10(6)Published in
European Journal of Biochemistry2004, volume: 271, number: 20, pages: 4107-4113
Publisher: BLACKWELL PUBLISHING LTD
Authors' information
Mowbray, Sherry
Swedish University of Agricultural Sciences, Department of Molecular Biosciences
Johansson, P
Henriksson, LM
Unge, T
Publication Identifiers
DOI: https://doi.org/10.1111/j.1432-1033.2004.04348.x
URI (permanent link to this page)
https://res.slu.se/id/publ/4824