5vwn | pdb_00005vwn

Triosephosphate isomerases deletion loop 3 from Trichomonas vaginalis

spinqualitylabelsall models 5vwn, resolution 1.74Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5vwn is a 1 chain structure with sequence from Trichomonas vaginalis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.74Å Ligands: NA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A2FT29_TRIV3 Publication Abstract from PubMed The protozoan parasite Trichomonas vaginalis contains two nearly identical triosephosphate isomerases (TvTIMs) that dissociate into stable monomers and dimerize upon substrate binding. Herein, we compare the role of the "ball and socket" and loop 3 interactions in substrate assisted dimer assembly in both TvTIMs. We found that point mutants at the "ball" are only 39 and 29-fold less catalytically active than their corresponding wild-type counterparts, whereas Deltaloop 3 deletions are 1502 and 9400-fold less active. Point and deletion mutants dissociate into stable monomers. However, point mutants assemble as catalytic competent dimers upon binding of the transition state substrate analog PGH, whereas loop 3 deletions remain monomeric. A comparison between crystal structures of point and loop 3 deletion monomeric mutants illustrates that the catalytic residues in point mutants and wild-type TvTIMs are maintained in the same orientation, whereas the catalytic residues in deletion mutants show an increase in thermal mobility and present structural disorder that may hamper their catalytic role. The high enzymatic activity present in monomeric point mutants correlates with the formation of dimeric TvTIMs upon substrate binding. In contrast, the low activity and lack of dimer assembly in deletion mutants suggests a role of loop 3 in promoting the formation of the active site as well as dimer assembly. Our results suggest that in TvTIMs the active site is assembled during dimerization and that the integrity of loop 3 and ball and socket residues is crucial to stabilize the dimer. A competent catalytic active site is necessary for substrate induced dimer assembly in triosephosphate isomerase.,Jimenez-Sandoval P, Vique-Sanchez JL, Hidalgo ML, Velazquez-Juarez G, Diaz-Quezada C, Arroyo-Navarro LF, Moran GM, Fattori J, Jessica Diaz-Salazar A, Rudino-Pinera E, Sotelo-Mundo R, Figueira ACM, Lara-Gonzalez S, Benitez-Cardoza CG, Brieba LG Biochim Biophys Acta. 2017 Nov;1865(11 Pt A):1423-1432. doi:, 10.1016/j.bbapap.2017.07.014. Epub 2017 Aug 9. PMID:28803140 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Triose phosphate isomerase 3D structures

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