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• W2021413720 abstract "Abstract Pantothenate synthetase (PS) catalyzes the final step of the pantothenate pathway, in which pantothenate is formed from pantoate and β‐alanine in an ATP‐dependent reaction. Mycobacterium tuberculosis PS (MTB PS) is functionally a dimer and a potential target for novel antitubercular drugs. Molecular dynamics simulations show that the functional dynamics of the enzyme are dominated by motions of a flexible gate loop in the N‐terminal domain and of the C‐terminal domain. The gate loop motions dominate in MTB PS while the C‐terminal domain motion dominates in Escherichia coli PS. Simulations also show that the correlated motions of the domains are severely compromised in the monomeric forms. Mutations that reduce the mobility of the gate loop in MTB PS and increased it in E. coli PS were designed and validated through simulations. Proteins 2011; © 2011 Wiley‐Liss, Inc." @default.
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• W2021413720 date "2011-03-21" @default.
• W2021413720 modified "2023-10-17" @default.
• W2021413720 title "A comparison of the dynamics of pantothenate synthetase from <i>M. tuberculosis</i> and <i>E. coli</i> : Computational studies" @default.
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• W2021413720 doi "https://doi.org/10.1002/prot.22994" @default.
• W2021413720 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/21425349" @default.
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