Discovery and evaluation of new compounds targeting ribosomal protein S1 in antibiotic-resistant Mycobacterium Tuberculosis

2020 ◽  
Vol 196 ◽  
pp. 112317
Author(s):  
Yazhuang Dai ◽  
Yinqiu Xu ◽  
Chenyun Guo ◽  
Xiaowen Xue ◽  
Donghai Lin ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Ribosomal Protein ◽  
Antibiotic Resistant ◽  
Ribosomal Protein S1 ◽  
New Compounds

1H, 15N, 13C resonance assignments for pyrazinoic acid binding domain of ribosomal protein S1 from Mycobacterium tuberculosis

2016 ◽  
Vol 10 (2) ◽  
pp. 321-324 ◽  
Author(s):  
Biling Huang ◽  
Jinglin Fu ◽  
Chenyun Guo ◽  
Xueji Wu ◽  
Donghai Lin ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Ribosomal Protein ◽  
Resonance Assignments ◽  
Binding Domain ◽  
Ribosomal Protein S1 ◽  
Pyrazinoic Acid

scholarly journals Mycobacterium tuberculosis ribosomal protein S1 (RpsA) and variants with truncated C-terminal end show absence of interaction with pyrazinoic acid

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Katherine Vallejos-Sánchez ◽  
Juan M. Lopez ◽  
Ricardo Antiparra ◽  
Emily Toscano ◽  
Harry Saavedra ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Ribosomal Protein ◽  
Ribosomal Protein S1 ◽  
Pyrazinoic Acid

Solution structure and backbone dynamics for S1 domain of ribosomal protein S1 from Mycobacterium tuberculosis

2019 ◽  
Vol 48 (6) ◽  
pp. 491-501 ◽  
Author(s):  
Biling Huang ◽  
Shihui Fan ◽  
Yan Liu ◽  
Yufen Zhao ◽  
Donghai Lin ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Ribosomal Protein ◽  
Solution Structure ◽  
Backbone Dynamics ◽  
Ribosomal Protein S1

Chemical shift assignments of Ribosomal protein S1 from Mycobacterium tuberculosis

2017 ◽  
Vol 11 (2) ◽  
pp. 133-136 ◽  
Author(s):  
Jinglin Fu ◽  
Biling Huang ◽  
Donghai Lin ◽  
Xinli Liao
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Chemical Shift ◽  
Ribosomal Protein ◽  
Chemical Shift Assignments ◽  
Ribosomal Protein S1

Lead compounds and key residues of ribosomal protein S1 in drug-resistant Mycobacterium tuberculosis

2019 ◽  
Vol 82 ◽  
pp. 58-67 ◽  
Author(s):  
Yunbao Zhi ◽  
Yazhuang Dai ◽  
Juanjuan Yang ◽  
Shuhua Tan ◽  
Donghai Lin ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Ribosomal Protein ◽  
Drug Resistant ◽  
Lead Compounds ◽  
Ribosomal Protein S1 ◽  
Key Residues

scholarly journals Structural Basis for the C-Terminal Domain of Mycobacterium tuberculosis Ribosome Maturation Factor RimM to Bind Ribosomal Protein S19

Biomolecules ◽  
2021 ◽  
Vol 11 (4) ◽  
pp. 597
Author(s):  
Haoran Zhang ◽  
Qiuxiang Zhou ◽  
Chenyun Guo ◽  
Liubin Feng ◽  
Huilin Wang ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Ribosomal Protein ◽  
Solution Structure ◽  
Molecular Mechanisms ◽  
Structural Model ◽  
Ribosomal Subunit ◽  
Structural Basis ◽  
Hydrophobic Core ◽  
Terminal Domain ◽  
Ribosomal Protein S19

Multidrug-resistant tuberculosis (TB) is a serious threat to public health, calling for the development of new anti-TB drugs. Chaperon protein RimM, involved in the assembly of ribosomal protein S19 into 30S ribosomal subunit during ribosome maturation, is a potential drug target for TB treatment. The C-terminal domain (CTD) of RimM is primarily responsible for binding S19. However, both the CTD structure of RimM from Mycobacterium tuberculosis (MtbRimMCTD) and the molecular mechanisms underlying MtbRimMCTD binding S19 remain elusive. Here, we report the solution structure, dynamics features of MtbRimMCTD, and its interaction with S19. MtbRimMCTD has a rigid hydrophobic core comprised of a relatively conservative six-strand β-barrel, tailed with a short α-helix and interspersed with flexible loops. Using several biophysical techniques including surface plasmon resonance (SPR) affinity assays, nuclear magnetic resonance (NMR) assays, and molecular docking, we established a structural model of the MtbRimMCTD–S19 complex and indicated that the β4-β5 loop and two nonconserved key residues (D105 and H129) significantly contributed to the unique pattern of MtbRimMCTD binding S19, which might be implicated in a form of orthogonality for species-dependent RimM–S19 interaction. Our study provides the structural basis for MtbRimMCTD binding S19 and is beneficial to the further exploration of MtbRimM as a potential target for the development of new anti-TB drugs.

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