Por favor, use este identificador para citar o enlazar este ítem:
http://ipicyt.repositorioinstitucional.mx/jspui/handle/1010/2085| A competent catalytic active site is necessary for substrate induced dimer assembly in triosephosphate isomerase | |
| Pedro Jiménez Sandoval JOSE LUIS VIQUE SANCHEZ MARISOL LOPEZ HIDALGO GILBERTO VELAZQUEZ JUAREZ Corina Diaz Quezada Luis Fernando Arroyo Navarro GABRIELA MARGARITA MONTERO MORAN Juliana Fattori ALMA JESSICA DIAZ SALAZAR ENRIQUE RUDIÑO PIÑERA ROGERIO RAFAEL SOTELO MUNDO Ana Carolina Figueira SAMUEL LARA GONZALEZ CLAUDIA GUADALUPE BENITEZ CARDOZA Luis G. Brieba | |
| Acceso Abierto | |
| Atribución-NoComercial-SinDerivadas | |
| https://doi.org/10.1016/j.bbapap.2017.07.014 | |
| Dimer assembly Triosephosphate isomerase Trichomonas X-ray crystallography | |
| "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 ?loop 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." | |
| Elsevier | |
| 2017 | |
| Artículo | |
| Pedro Jimenez-Sandoval, Jose Luis Vique-Sanchez, Marisol López Hidalgo, Gilberto Velazquez-Juarez, Corina Diaz-Quezada, Luis Fernando Arroyo-Navarro, Gabriela Montero Moran, Juliana Fattori, A. Jessica Diaz-Salazar, Enrique Rudiño-Pinera, Rogerio Sotelo-Mundo, Ana Carolina Migliorini Figueira, Samuel Lara-Gonzalez, Claudia G. Benítez-Cardoza, Luis G. Brieba, A competent catalytic active site is necessary for substrate induced dimer assembly in triosephosphate isomerase, Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, Volume 1865, Issue 11, Part A, 2017, Pages 1423-1432. | |
| BIOLOGÍA MOLECULAR | |
| Versión aceptada | |
| acceptedVersion - Versión aceptada | |
| Aparece en las colecciones: | Publicaciones Científicas Biología Molecular |
Cargar archivos:
| Fichero | Tamaño | Formato | |
|---|---|---|---|
| BiochimBiophysActa1865(2017)1423.pdf | 2.04 MB | Adobe PDF | Visualizar/Abrir |