scholarly journals The NMR solution structure of Mycobacterium tuberculosis F‐ ATP synthase subunit ε provides new insight into energy coupling inside the rotary engine

FEBS Journal ◽  
2018 ◽  
Vol 285 (6) ◽  
pp. 1111-1128 ◽  
Author(s):  
Shin Joon ◽  
Priya Ragunathan ◽  
Lavanya Sundararaman ◽  
Wilson Nartey ◽  
Subhashri Kundu ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Atp Synthase ◽  
Solution Structure ◽  
Energy Coupling ◽  
Nmr Solution Structure ◽  
Rotary Engine ◽  
Insight Into

scholarly journals NMR solution structure of tricyclo-DNA containing duplexes: insight into enhanced thermal stability and nuclease resistance

2019 ◽  
Vol 47 (9) ◽  
pp. 4872-4882 ◽  
Author(s):  
Andrei Istrate ◽  
Silke Johannsen ◽  
Alena Istrate ◽  
Roland K O Sigel ◽  
Christian J Leumann
Keyword(s):  
Thermal Stability ◽  
Solution Structure ◽  
Nmr Solution Structure ◽  
Nuclease Resistance ◽  
Insight Into

Solution structure of subunit γ (γ1-204) of the Mycobacterium tuberculosis F-ATP synthase and the unique loop of γ165-178, representing a novel TB drug target

2012 ◽  
Vol 45 (1-2) ◽  
pp. 121-129 ◽  
Author(s):  
Ragunathan Priya ◽  
Goran Biuković ◽  
Malathy Sony Subramanian Manimekalai ◽  
Jackwee Lim ◽  
Srinivasa P. S. Rao ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Atp Synthase ◽  
Drug Target ◽  
Solution Structure

scholarly journals Variations of Subunit ε of the Mycobacterium tuberculosis F1FoATP Synthase and a Novel Model for Mechanism of Action of the Tuberculosis Drug TMC207

2012 ◽  
Vol 57 (1) ◽  
pp. 168-176 ◽  
Author(s):  
Goran Biuković ◽  
Sandip Basak ◽  
Malathy Sony Subramanian Manimekalai ◽  
Sankaranarayanan Rishikesan ◽  
Manfred Roessle ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Atp Synthase ◽  
Solution Structure ◽  
Helical Structure ◽  
Terminal Segment ◽  
New Drugs ◽  
Drug Candidate ◽  
Content Type ◽  
Arginine Residues ◽  
Coupling Processes

ABSTRACTThe subunit ε of bacterial F1FOATP synthases plays an important regulatory role in coupling and catalysis via conformational transitions of its C-terminal domain. Here we present the first low-resolution solution structure of ε ofMycobacterium tuberculosis(Mtε) F1FOATP synthase and the nuclear magnetic resonance (NMR) structure of its C-terminal segment (Mtε103–120).Mtε is significantly shorter (61.6 Å) than forms of the subunit in other bacteria, reflecting a shorter C-terminal sequence, proposed to be important in coupling processes via the catalytic β subunit. The C-terminal segment displays an α-helical structure and a highly positive surface charge due to the presence of arginine residues. Using NMR spectroscopy, fluorescence spectroscopy, and mutagenesis, we demonstrate that the new tuberculosis (TB) drug candidate TMC207, proposed to bind to the proton translocatingc-ring, also binds toMtε. A model for the interaction of TMC207 with both ε and thec-ring is presented, suggesting that TMC207 forms a wedge between the two rotating subunits by interacting with the residues W15 and F50 of ε and thec-ring, respectively. T19 and R37 of ε provide the necessary polar interactions with the drug molecule. This new model of the mechanism of TMC207 provides the basis for the design of new drugs targeting the F1FOATP synthase inM. tuberculosis.

scholarly journals Domain Features of the Peripheral Stalk Subunit H of the Methanogenic A1AO ATP Synthase and the NMR Solution Structure of H1-47

2009 ◽  
Vol 97 (1) ◽  
pp. 286-294 ◽  
Author(s):  
Goran Biuković ◽  
Shovanlal Gayen ◽  
Konstantin Pervushin ◽  
Gerhard Grüber
Keyword(s):  
Atp Synthase ◽  
Solution Structure ◽  
Nmr Solution Structure ◽  
Peripheral Stalk ◽  
A1ao Atp Synthase

scholarly journals Insight into the HIV-1 Vif SOCS-box–ElonginBC interaction

Open Biology ◽  
2013 ◽  
Vol 3 (11) ◽  
pp. 130100 ◽  
Author(s):  
Zhisheng Lu ◽  
Julien R. C. Bergeron ◽  
R. Andrew Atkinson ◽  
Torsten Schaller ◽  
Dennis A. Veselkov ◽  
...  
Keyword(s):  
Solution Structure ◽  
Hydrophobic Interactions ◽  
Dynamic Information ◽  
Ubiquitin Ligase Complex ◽  
Biophysical Studies ◽  
Viral Infectivity Factor ◽  
Β Sheet ◽  
Socs Box ◽  
Insight Into ◽  
Hiv 1

The HIV-1 viral infectivity factor (Vif) neutralizes cell-encoded antiviral APOBEC3 proteins by recruiting a cellular ElonginB (EloB)/ElonginC (EloC)/Cullin5-containing ubiquitin ligase complex, resulting in APOBEC3 ubiquitination and proteolysis. The suppressors-of-cytokine-signalling-like domain (SOCS-box) of HIV-1 Vif is essential for E3 ligase engagement, and contains a BC box as well as an unusual proline-rich motif. Here, we report the NMR solution structure of the Vif SOCS–ElonginBC (EloBC) complex. In contrast to SOCS-boxes described in other proteins, the HIV-1 Vif SOCS-box contains only one α-helical domain followed by a β-sheet fold. The SOCS-box of Vif binds primarily to EloC by hydrophobic interactions. The functionally essential proline-rich motif mediates a direct but weak interaction with residues 101–104 of EloB, inducing a conformational change from an unstructured state to a structured state. The structure of the complex and biophysical studies provide detailed insight into the function of Vif's proline-rich motif and reveal novel dynamic information on the Vif–EloBC interaction.

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.

Sign in / Sign up

Export Citation Format

Share Document