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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Mishra, Vibhor Kumar, Ashutosh Ali, Vahab Zhang, Kam Y. J. Nozaki, Tomoyoshi |
| Description | Author Affiliation: Mishra V ( Division of Molecular and Structural Biology, Central Drug Research Institute, Lucknow 226031, India. Electronic address: mishravibhor@gmail.com.); Kumar A ( Structural Bioinformatics Team, Division of Structural and Synthetic Biology, Center for Life Science Technologies, RIKEN, 1-7-22 Suehiro, Yokohamo 2300045, Kanagawa, Japan.); Ali V ( Laboratory of Molecular Biochemistry and Cell Biology, Department of Biochemistry, Rajendra Memorial Research Institute of Medical Sciences, Agam Kuan, Patna, India.); Zhang KY ( Structural Bioinformatics Team, Division of Structural and Synthetic Biology, Center for Life Science Technologies, RIKEN, 1-7-22 Suehiro, Yokohamo 2300045, Kanagawa, Japan.); Nozaki T ( Department of Parasitology, National Institute of Infectious diseases, 1-23-1 Toyama, Shinjuku-Ku, Tokyo 162-8640, Japan.) |
| Abstract | Entamoeba histolytica D-phosphoglycerate dehydrogenase (EhPGDH) exists as a functionally active homodimer at pH 7. Our earlier studies have shown that ionic interactions are essentially required for the oligomeric status and activity of the protein. Present study focuses on pH associated structural modulations of EhPGDH. Far-UV CD spectra showed loss in the secondary structure of the protein as a function of low pH, however, the protein was not completely unfolded even at pH 2. Energy minimized average simulated models of EhPGDH at different pH show stable secondary structure elements in the nucleotide binding domain (NBD) however, the substrate binding domain (SBD) was more sensitive toward acidic pH and completely unfolds at pH 2. The data suggest presence of partially folded/unfolded intermediate state at pH 2. Size exclusion chromatography shows that this intermediate has larger hydrodynamic radius compared with dimer (pH 7) or monomer (pH 5). The intermediate has poor tertiary organization with significantly exposed hydrophobic patches monitored by pH-dependent fluorescence spectroscopy and molecular dynamic simulations. Collectively, the results suggest that the two domains (NBD and SBD) of EhPGDH have independent pH-dependent structural transitions with stabilization of an intermediate state at pH 2. |
| File Format | HTM / HTML |
| ISSN | 01418130 |
| Volume Number | 79 |
| e-ISSN | 18790003 |
| Journal | International Journal of Biological Macromolecules |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2015-08-01 |
| Publisher Place | Netherlands |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Discipline Biochemistry Entamoeba Histolytica Enzymology Phosphoglycerate Dehydrogenase Chemistry Protozoan Proteins Genetics Gene Expression Hydrogen-ion Concentration Kinetics Molecular Dynamics Simulation Isolation & Purification Protein Folding Protein Multimerization Protein Stability Protein Structure, Secondary Protein Structure, Tertiary Thermodynamics Journal Article Research Support, Non-u.s. Gov't |
| Content Type | Text |
| Resource Type | Article |
| Subject | Structural Biology Molecular Biology Biochemistry |
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