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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Mahmood, Anjum Arora, Ashish Ramachandran, Ravishankar Luthra, Amit |
| Description | Author Affiliation: Luthra A ( Molecular and Structural Biology Division, Central Drug Research Institute, P.O. Box 173, Chattar Manzil, Mahatma Gandhi Marg, Lucknow-226001, India.) |
| Abstract | Rv3868, a conserved hypothetical protein of the ESAT-6 secretion system of Mycobacterium tuberculosis, is essential for the secretion of at least four virulence factors. Each protein chain is approximately 63 kDa and assembles into a hexamer. Limited proteolysis demonstrates that it consists of two domains joined by a linker. The N-terminal domain is a compact, helical domain of approximately 30 kDa and apparently functions to regulate the ATPase activity of the C-terminal domain and the oligomerization. The nucleotide binding site is situated in the C-terminal domain, which exhibits ATP-dependent self-association. It is also the oligomerization domain. Dynamic fluorescence quenching studies demonstrate that the domain is proximal to the C terminus in the apoprotein and exhibits a specific movement upon ATP binding. In silico modeling of the domains suggests that Arg-429 of a neighboring subunit forms a part of the binding site upon oligomerization. Mutational analysis of binding site residues demonstrates that the Arg-429 functions as the important 'sensor arginine' in AAA-ATPases. Protein NMR experiments involving CFP-10 and activity assays rule out a general chaperone-like function for Rv3868. On the other hand, ATP-dependent 'open-close' movements of the individual domains apparently enable it to interact and transfer energy to co-proteins in the ESX-1 pathway. |
| ISSN | 00219258 |
| e-ISSN | 1083351X |
| Journal | Journal of Biological Chemistry |
| Issue Number | 52 |
| Volume Number | 283 |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date | 2008-12-26 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Adenosine Triphosphatases Chemistry Bacterial Proteins Gene Expression Regulation, Bacterial Mycobacterium Tuberculosis Metabolism Adenosine Triphosphate Arginine Binding Sites DNA Mutational Analysis Magnetic Resonance Spectroscopy Microscopy, Fluorescence Molecular Chaperones Phylogeny Protein Binding Protein Structure, Tertiary Spectrometry, Mass, Electrospray Ionization Research Support, Non-U.S. Gov't Biochemistry Molecular Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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