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Molecular Dynamics Simulations of the FtsZ mutant G105S

View ORCID ProfileVidyalakshmi C Muthukumar
doi: https://doi.org/10.1101/280248
Vidyalakshmi C Muthukumar
aDepartment of Chemistry, University of Warwick
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Abstract

In our previous studies we simulated FtsZ monomer and dimer in different nucleotide binding states. In our simulations, we had used the E.coli FtsZ homology model including the FtsZ Intrinsically Disordered Region (IDR). Our simulations revealed that FtsZ dynamics involves a key stage in which GTP binds to monomeric FtsZ and opens its nucleotide binding site which in turn favours polymerization. During dimerization, the C-terminal of the top monomer rotates considerably towards the bottom monomer. Such a rotation of the C-terminal domain leads to capture of the nucleotide by its N-terminal domain. In this study we simulate the FtsZ G105S mutant to see if it may have ATPase activity which was reported in a previous study.

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Posted March 11, 2018.
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Molecular Dynamics Simulations of the FtsZ mutant G105S
Vidyalakshmi C Muthukumar
bioRxiv 280248; doi: https://doi.org/10.1101/280248
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Molecular Dynamics Simulations of the FtsZ mutant G105S
Vidyalakshmi C Muthukumar
bioRxiv 280248; doi: https://doi.org/10.1101/280248

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