Your browser doesn't support javascript.
loading
Engineering a calcium-dependent conformational change in Calbindin D9k by secondary elements replacement.
Arévalo-Salina, Emma L; Osuna, Joel; Flores, Humberto; Saab-Rincon, Gloria.
Affiliation
  • Arévalo-Salina EL; Departamento Ingeniería Celular y Biocatálisis, Instituto de Biotecnología, Universidad Nacional Autónoma de México, Apartado Postal 510-3, Cuernavaca, Morelos, 62250, Mexico.
  • Osuna J; Departamento Ingeniería Celular y Biocatálisis, Instituto de Biotecnología, Universidad Nacional Autónoma de México, Apartado Postal 510-3, Cuernavaca, Morelos, 62250, Mexico.
  • Flores H; Departamento Ingeniería Celular y Biocatálisis, Instituto de Biotecnología, Universidad Nacional Autónoma de México, Apartado Postal 510-3, Cuernavaca, Morelos, 62250, Mexico.
  • Saab-Rincon G; Departamento Ingeniería Celular y Biocatálisis, Instituto de Biotecnología, Universidad Nacional Autónoma de México, Apartado Postal 510-3, Cuernavaca, Morelos, 62250, Mexico. Electronic address: gloria.saab@ibt.unam.mx.
Arch Biochem Biophys ; 714: 109065, 2021 12 15.
Article in En | MEDLINE | ID: mdl-34710387
EF-hand is a common motif in Ca2+-binding proteins, some of which present a conformational change upon Ca2+-binding, a relevant property for signal transduction. In the present work, we investigated the behavior of Calbindin D9k, a modulator protein with a high affinity for Ca2+ but structurally insensitive to its presence. Its non-canoncal N-terminal EF-hand was replaced by chimeric motifs, containing increasing structural elements from the sensor troponin C SCIII motif. We demonstrated that the loop and helix II were the necessary elements for a conformational change promoted by calcium in chimeric Calbindin D9k. Fusion of the isolated chimeric motifs to an activity reporter gene showed the loop as the minimal element to promote a conformational change. The discrepancy between these results is discussed in the light of inter-motif interactions and helix I participation in modulating the Ca2+ affinity and restricting motif conformation.
Subject(s)
Key words

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: S100 Calcium Binding Protein G / Calcium Type of study: Prognostic_studies Language: En Journal: Arch Biochem Biophys Year: 2021 Document type: Article Affiliation country: Mexico Country of publication: United States

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: S100 Calcium Binding Protein G / Calcium Type of study: Prognostic_studies Language: En Journal: Arch Biochem Biophys Year: 2021 Document type: Article Affiliation country: Mexico Country of publication: United States