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| Title | High-Resolution Structure of ClpC1-Rufomycin and Ligand Binding Studies Provide a Framework to Design and Optimize Anti-Tuberculosis Leads. |
|---|---|
| Journal, issue, pages | Acs Infect Dis., Vol. 5, Page 829-840, Year 2019 |
| Publish date | Mar 7, 2018 (structure data deposition date) |
Authors | Wolf, N.M. / Lee, H. / Choules, M.P. / Pauli, G.F. / Phansalkar, R. / Anderson, J.R. / Gao, W. / Ren, J. / Santarsiero, B.D. / Cheng, J. ...Wolf, N.M. / Lee, H. / Choules, M.P. / Pauli, G.F. / Phansalkar, R. / Anderson, J.R. / Gao, W. / Ren, J. / Santarsiero, B.D. / Cheng, J. / Jin, Y.Y. / Ho, N.A. / Duc, N.M. / Suh, J.W. / Abad-Zapatero, C. / Cho, S. |
External links | Acs Infect Dis. / PubMed:30990022 |
| Methods | X-ray diffraction |
| Resolution | 1.4 Å |
| Structure data | ![]() PDB-6cn8: |
| Chemicals | ![]() ChemComp-PO4: ![]() ChemComp-CL: ![]() ChemComp-NA: ![]() ChemComp-HOH: |
| Source |
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Keywords | CHAPERONE/ANTIBIOTIC / Mycobacterium tuberculosis / rufomycin I / macrocyclic peptide / ClpC1-NTD / Chaperone / ATP-dependent protease / CHAPERONE-ANTIBIOTIC complex / ATPase AAA+ / natural product |
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