Structure of C-terminal Domain of Peptidyl-prolyl cis-trans Isomerase from Pseudomonas syringae pv. Tomato str. DC3000 at 1.6Å Resolution

Title:Structure of C-terminal Domain of Peptidyl-prolyl cis-trans Isomerase from Pseudomonas syringae pv. Tomato str. DC3000 at 1.6Å Resolution

Volume: 24 Issue: 6

Author(s): Yu Gao, Hong-mei Zhang, Pi-wu Wang*Mei Li*

Affiliation:

• College of Agronomy, Jilin Agricultural University. No.2888 Xincheng Street, Changchun, Jilin,China

• National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Chaoyang District, Beijing 100101,China

Keywords: FKBP, PPIase, crystal structure, MIP, FK506, rapamycin.

Abstract: Background: Peptidyl-prolyl cis-trans isomerase (PPIase) accelerates the intrinsically slow conversion between cis- and trans- configurations of proline, thus affecting backbone conformation and altering the direction of peptide chains. PPIase from Pseudomonas syringae pv. Tomato (PSPTO) DC3000 (PSPTO-PPIase) is considered to belong to the FKBP subfamily of PPIase.

Objective: To solve the high resolution structure of the PSPTO-PPIase, and to explore its potential function in plants pathogen PSPTO DC3000.

Method: The PSPTO-PPIase was expressed in E.coli and purified through ion exchange and size exclusion chromatography. While only the C-terminal domain of PSPTO-PPIase was successfully crystalized, and its structure was solved to 1.6 Å resolution by molecular replacement method.

Results: Structural comparison showed that PSPTO-PPIase adopts a similar overall fold with microphage infectivity potentiators (MIPs), which also belong to the FKBP subfamily of PPIase. In addition, the BIAcore result confirmed that PSPTO-PPIase can bind an immunosuppressive drug FK506 as some other FKBP subfamily members do.

Conclusion: Our results suggested that PSPTO-PPIase may function in a similar manner to virulent factor MIPs during pathogenesis. And the immunosuppressive drugs FK506 and rapamycin binding to PSPTO-PPIase potentially interferes and inhibits the plant pathogen PSPTO DC3000. In addition, the amino acids with short side chains in the fourth loop (L4) of PSPTO-PPIase may account for its variable roles in the respective pathogen.

Cite this article as:

Gao Yu , Zhang Hong-mei , Wang Pi-wu *, Li Mei *, Structure of C-terminal Domain of Peptidyl-prolyl cis-trans Isomerase from Pseudomonas syringae pv. Tomato str. DC3000 at 1.6Å Resolution, Protein & Peptide Letters 2017; 24 (6) . https://dx.doi.org/10.2174/0929866524666170414093308

DOI https://dx.doi.org/10.2174/0929866524666170414093308	Print ISSN 0929-8665
Publisher Name Bentham Science Publisher	Online ISSN 1875-5305