Mutational effects on structural stability of SRP pathway dependent co-translational protein ftsY of Mycobacterium tuberculosis H37Rv

Shivangi, .; Beg, Amjad; Meena, Laxman S.

doi:10.1016/j.genrep.2019.100395

Cited by 17 publications

(14 citation statements)

References 29 publications

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“…The predicted destability value mostly destabilizing on positioned Aspartate into Alanine -0.583 kcal/mol and Aspartate into Glycine -0.379 kcal/mol. Here, Aspartate into Alanine (ASP175ALA) mutation predicted as the most destabilizing and it will destabilize the protein conformation (see Figure 8) [45][46][47]. As many studies already revealed the importance of ATP binding genes in various biological processes of living organisms, thus this work delivers importance of Rv1463 as different and interesting part for understanding the molecular mechanism of survival of this bacterium.…”

Section: Structural Based Mutation-induced Stability Deviationsmentioning

confidence: 93%

MOLECULAR BASIS AND INTEGRATIVE ANALYSIS OF Rv1463 AS PROBABLE CONSERVED ATP-BINDING PROTEIN BY COMPUTATIONAL APPROACH

Beg¹,

Sevindik²,

Haider³

et al. 2021

Ankara Universitesi Eczacilik Fakultesi Dergisi

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Objective: Tuberculosis as a global epidemic since years due to vigorously changing dynamics of its causal pathogen, Mycobacterium tuberculosis H37Rv (M. tuberculosis). This pathogen has worsened the situation therefore making it so challenging and hard to overcome. In this manuscript, we have used the computational approaches for ATP-binding protein of Mycobacterium tuberculosis H37Rv (M. tuberculosis) that helps in transportation of metal ion across the plasma membranes and resultant generating an electrochemical gradient. Rv1463 a hypothetical protein possessing ATP binding motif (WalkerA) (GXXXXGKS/T), and (Walker B) (DEXXXXXD) and significance of these motifs in ATP binding and hydrolyzing activities. It shows the ATP-binding property by interacting with transcriptional regulatory protein and showing the interacted compounds as magnesium (Mg) and Adenosine di phosphate (ADP).Material and Method: The structure of Rv1463 has been build by the Swiss Model webserver and molecular docking was done using AutoDock.

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Section: Structural Based Mutation-induced Stability Deviationsmentioning

confidence: 93%

MOLECULAR BASIS AND INTEGRATIVE ANALYSIS OF Rv1463 AS PROBABLE CONSERVED ATP-BINDING PROTEIN BY COMPUTATIONAL APPROACH

Beg¹,

Sevindik²,

Haider³

et al. 2021

Ankara Universitesi Eczacilik Fakultesi Dergisi

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show abstract

“…It also includes data for mycobacterial structure, function, orthologs and all information regarding drug development. The protein sequence was used for determination of GTPase and pyrophosphatase active site motif [34].…”

Section: Active Site Analysis and Residues Selectionmentioning

confidence: 99%

Biophysical and Computational Landscapes of Mycobacterial Pyrophosphatase: A Closer View of Drug Repurposing With Different Natural and Synthetic Compounds.

Shivangi

Meena

2021

Preprint

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Mycobacterial pyrophosphatase (Mt-ppa) play essential role in bacterial in vitro and in vivo survival. This family of proteins reacts on pyrophosphates to release orthophosphates and protect bacteria from pyrophosphates toxicity. Rv3628 encodes pyrophosphate protein which is a type I pyrophosphate protein. This protein is engaged in hydrolysis of tri and diphosphates (majorly GTP, ATP and GDP) and its catalysis is metal ion dependent. Mt-ppa was showed efficient interaction with GTP molecule, whose Kd was 37.9µM, ΔH was -11Kcal/mol and ΔG was -6.06Kcal/mol. The protein was interacted with ATP family genes that resemble that it is participator in conversion of diphosphates moiety to the residual monophosphates. W102G, V150G, F44G, I119G, L93F, F3G, F122G, I108G, L32G, M82G, Y17G, L59G, V5G, V26G, I7G, W140D, W140G, W140A, F80G, W140S, L49G, L56G, I9G, V60G, V19G, V92G, L28G, L61G, Y126E and F123G are the top 30 mutation hits and Y126G, Y42G, R30G, E8G, K16G are top mutational hits in active site of Mt-ppa. Mt-ppa is temperature and pH sensitive as increasing temperature and pH decreases protein stability. It is also the receptor for several kinases that phosphorylate this protein at different Ser/Thr/Tyr sites. Virtual screening of 700 compounds from herbal ingredient targets (HITs) subset of zinc database give ZINC000003979028, ZINC000003870413, ZINC000003870412, ZINC000150338758, ZINC0000070450948, ZINC000150338754, ZINC000095098891, ZINC000000119985, ZINC000005085286 as the top target hits and Mac0182344 and NAV_2729 as the top GTPase inhibitor that can target and hinders Mt-ppa activity.

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“…36 Further, binding analysis using the visualization approach was carried out to understand the binding pattern of the drug with protein. [37][38][39][40][41] Result and discussion…”

Section: Interaction Analysis: Visualization and Evaluationmentioning

confidence: 99%

Anti-HIV and Anti-HCV drugs are the putative inhibitors of RNA-dependent-RNA polymerase activity of NSP12 of the SARS CoV-2 (COVID-19)

Athar¹,

Beg²

2020

PPIJ

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Mutational effects on structural stability of SRP pathway dependent co-translational protein ftsY of Mycobacterium tuberculosis H37Rv

Cited by 17 publications

References 29 publications

MOLECULAR BASIS AND INTEGRATIVE ANALYSIS OF Rv1463 AS PROBABLE CONSERVED ATP-BINDING PROTEIN BY COMPUTATIONAL APPROACH

MOLECULAR BASIS AND INTEGRATIVE ANALYSIS OF Rv1463 AS PROBABLE CONSERVED ATP-BINDING PROTEIN BY COMPUTATIONAL APPROACH

Biophysical and Computational Landscapes of Mycobacterial Pyrophosphatase: A Closer View of Drug Repurposing With Different Natural and Synthetic Compounds.

Anti-HIV and Anti-HCV drugs are the putative inhibitors of RNA-dependent-RNA polymerase activity of NSP12 of the SARS CoV-2 (COVID-19)

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