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X-ray structure of peptidyl-prolyl cis-trans isomerase A from Mycobacterium tuberculosis.

Henriksson LM, Johansson P, Unge T, Mowbray SL
Eur J Biochem 271 4107-13 (2004)
Cited: 11 times
EuropePMC logo PMID: 15479239

Abstract

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 kcat/Km of 2.0 x 10(6) m(-1).s(-1). The X-ray structure of PpiA was solved by molecular replacement, and refined to a resolution of 2.6 A with R and Rfree values of 21.3% and 22.9%, respectively. Comparisons to known structures show that the PpiA represents a slight variation on the peptidyl-prolyl cis-trans isomerase fold, previously not represented in the Protein Data Bank. Inspection of the active site suggests that specificity for substrates and cyclosporin A will be similar to that found for most other enzymes of this structural family. Comparison to the sequence of the second M. tuberculosis enzyme, PpiB, suggests that binding of peptide substrates as well as cyclosporin A may differ in that case.

Articles - 1w74 mentioned but not cited (3)

  1. Systematic Analysis of Mycobacterial Acylation Reveals First Example of Acylation-mediated Regulation of Enzyme Activity of a Bacterial Phosphatase. Singhal A, Arora G, Virmani R, Kundu P, Khanna T, Sajid A, Misra R, Joshi J, Yadav V, Yadav V, Samanta S, Saini N, Pandey AK, Visweswariah SS, Hentschker C, Becher D, Gerth U, Singh Y. J Biol Chem 290 26218-26234 (2015)
  2. Mycobacterium tuberculosis cyclophilin A uses novel signal sequence for secretion and mimics eukaryotic cyclophilins for interaction with host protein repertoire. Bhaduri A, Misra R, Maji A, Bhetaria PJ, Mishra S, Arora G, Singh LK, Dhasmana N, Dubey N, Virdi JS, Singh Y. PLoS One 9 e88090 (2014)
  3. Mycobacterium tuberculosis Peptidyl-Prolyl Isomerases Also Exhibit Chaperone like Activity In-Vitro and In-Vivo. Pandey S, Sharma A, Tripathi D, Kumar A, Khubaib M, Bhuwan M, Chaudhuri TK, Hasnain SE, Ehtesham NZ. PLoS One 11 e0150288 (2016)


Reviews citing this publication (1)

  1. Microbial cyclophilins: specialized functions in virulence and beyond. Dimou M, Venieraki A, Katinakis P. World J Microbiol Biotechnol 33 164 (2017)

Articles citing this publication (7)

  1. Assessment of live candidate vaccines for paratuberculosis in animal models and macrophages. Scandurra GM, de Lisle GW, Cavaignac SM, Young M, Kawakami RP, Collins DM. Infect Immun 78 1383-1389 (2010)
  2. The crystal structure of Aspergillus fumigatus cyclophilin reveals 3D domain swapping of a central element. Limacher A, Kloer DP, Flückiger S, Folkers G, Crameri R, Scapozza L. Structure 14 185-195 (2006)
  3. Cytosolic Proteome Profiling of Aminoglycosides Resistant Mycobacterium tuberculosis Clinical Isolates Using MALDI-TOF/MS. Sharma D, Lata M, Singh R, Deo N, Venkatesan K, Bisht D. Front Microbiol 7 1816 (2016)
  4. Mycobacterium tuberculosis Peptidyl-Prolyl Isomerases Are Immunogenic, Alter Cytokine Profile and Aid in Intracellular Survival. Pandey S, Tripathi D, Khubaib M, Kumar A, Sheikh JA, Sumanlatha G, Ehtesham NZ, Hasnain SE. Front Cell Infect Microbiol 7 38 (2017)
  5. Structural and biochemical characterization of the cytosolic wheat cyclophilin TaCypA-1. Sekhon SS, Kaur H, Dutta T, Singh K, Kumari S, Kang S, Park SG, Park BC, Jeong DG, Pareek A, Woo EJ, Singh P, Yoon TS. Acta Crystallogr D Biol Crystallogr 69 555-563 (2013)
  6. Cyclosporin A binding to Mycobacterium tuberculosis peptidyl-prolyl cis-trans isomerase A--investigation by CD, FTIR and fluorescence spectroscopy. Mitra D, Mukherjee S, Das AK. FEBS Lett 580 6846-6860 (2006)
  7. Actinobacteria cyclophilins: phylogenetic relationships and description of new class- and order-specific paralogues. Manteca A, Pelaez AI, Zardoya R, Sanchez J. J Mol Evol 63 719-732 (2006)


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