PDBsum entry 5yb9

Isomerase

PDB id: 5yb9

Contents

Protein chain

172 a.a.

Waters ×47

PDB id:

5yb9

Name:

Isomerase

Title:

Crystal structure of a dimeric cyclophilin a from t.Vaginalis

Structure:

Peptidyl-prolyl cis-trans isomerase. Chain: a. Synonym: ppiase. Engineered: yes. Other_details: cyclophilin a

Source:

Trichomonas vaginalis. Organism_taxid: 5722. Gene: tvag_004440. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Resolution:

2.28Å R-factor: 0.219 R-free: 0.286

Authors:

C.C.Cho,M.H.Lin,C.C.Chou,T.Martin,C.Chen,C.H.Hsu

Key ref:

T.Martin et al. (2018). Structural basis of interaction between dimeric cyclophilin 1 and Myb1 transcription factor in Trichomonas vaginalis. Sci Rep, 8, 5410. PubMed id: 29615721

Date:

04-Sep-17 Release date: 18-Jul-18

Protein chain

A2DT06  (A2DT06_TRIVA) -  Peptidyl-prolyl cis-trans isomerase from Trichomonas vaginalis (strain ATCC PRA-98 / G3)

Seq: 173 a.a.

Struc: 172 a.a.

Enzyme reactions

• Enzyme class: E.C.5.2.1.8 - peptidylprolyl isomerase.
• Reaction: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

Added reference

Sci Rep 8:5410 (2018)

PubMed id: 29615721

Structural basis of interaction between dimeric cyclophilin 1 and Myb1 transcription factor in Trichomonas vaginalis.

T.Martin, Y.C.Lou, C.C.Chou, S.Y.Wei, S.Sadotra, C.C.Cho, M.H.Lin, J.H.Tai, C.H.Hsu, C.Chen.

ABSTRACT

Cyclophilin 1 (TvCyP1), a cyclophilin type peptidyl-prolyl isomerase present in the human parasite Trichomonas vaginalis, interacts with Myb1 and assists in its nuclear translocation. Myb1 regulates the expression of ap65-1 gene that encodes for a disease causing cytoadherence enzyme. Here, we determined the crystal structures of TvCyP1 and its complex with the minimum TvCyP1-binding sequence of Myb1 (Myb1^104-111), where TvCyP1 formed a homodimer, unlike other single domain cyclophilins. In the complex structure, one Myb1^104-111 peptide was bound to each TvCyP1 protomer, with G106-P107 and Y105 fitting well into the active site and auxiliary S2 pocket, respectively. NMR data further showed that TvCyP1 can catalyze the cis/trans isomerization of P107 in Myb1^104-111. Interestingly, in the well-folded Myb1 protein (Myb1^35-141), the minimum binding sequence adopted a different conformation from that of unstructured Myb1^104-111 peptide, that could make P107 binding to the active site of TvCyP1 difficult. However, NMR studies showed that similar to Myb1^104-111 peptide, Myb1^35-141 also interacted with the active site of TvCyP1 and the dynamics of the Myb1^35-141 residues near P107 was reduced upon interaction. Together, the structure of TvCyP1 and detailed structural insights on TvCyP1-Myb1 interaction provided here could pave the way for newer drugs to treat drug-resistant strains.