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TitleThermodynamic and kinetic analysis of the LAO binding protein and its isolated domains reveal non-additivity in stability, folding and function.
Journal, issue, pagesFebs J., Year 2023
Publish dateJun 27, 2020 (structure data deposition date)
AuthorsVergara, R. / Berrocal, T. / Juarez Mejia, E.I. / Romero-Romero, S. / Velazquez-Lopez, I. / Pulido, N.O. / Lopez Sanchez, H.A. / Silva, D.A. / Costas, M. / Rodriguez-Romero, A. ...Vergara, R. / Berrocal, T. / Juarez Mejia, E.I. / Romero-Romero, S. / Velazquez-Lopez, I. / Pulido, N.O. / Lopez Sanchez, H.A. / Silva, D.A. / Costas, M. / Rodriguez-Romero, A. / Rodriguez-Sotres, R. / Sosa-Peinado, A. / Fernandez-Velasco, D.A.
External linksFebs J. / PubMed:37178351
MethodsX-ray diffraction
Resolution2.4 Å
Structure data

PDB-6xks:
Crystal structure of domain A from the periplasmic Lysine-, Arginine-, Ornithine-binding protein (LAO) of Salmonella typhimurium
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

Chemicals

ChemComp-ACT:
ACETATE ION

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-HOH:
WATER

Source
  • salmonella typhimurium (bacteria)
KeywordsPROTEIN BINDING / Periplasmic Binding Protein / LAO / Protein folding / Thermodynamics / Kinetics

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