Conformational changes and binding property of the periplasmic binding protein BtuF during vitamin B12 transport revealed by collision-induced unfolding, hydrogen-deuterium exchange mass spectrometry and molecular dynamic simulation-Reference-Cited by-同舟云学术

Conformational changes and binding property of the periplasmic binding protein BtuF during vitamin B12 transport revealed by collision-induced unfolding, hydrogen-deuterium exchange mass spectrometry and molecular dynamic simulation

Published:2021-09 Issue: Volume:187 Page:350-360
ISSN:0141-8130
Container-title:International Journal of Biological Macromolecules
language:en
Short-container-title:International Journal of Biological Macromolecules

Author:

Zhou Lijun,Wang Defu,Iftikhar Mehwish,Lu Yinghong,Zhou Min

Publisher

Elsevier BV

Subject

Molecular Biology,General Medicine,Biochemistry,Structural Biology

Reference61 articles.

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2. The E. coli BtuCD structure: a framework for ABC transporter architecture and mechanism;Locher;Science,2002

3. Crystal structures of the BtuF periplasmic-binding protein for vitamin B12 suggest a functionally important reduction in protein mobility upon ligand binding;Karpowich;J. Biol. Chem.,2003

4. Ligand binding specificity of the Escherichia coli periplasmic histidine binding protein, HisJ;Paul;Protein Sci.,2017

5. Periplasmic binding protein dimer has a second allosteric event tied to ligand binding;Li;Biochemistry,2017

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