Please use this identifier to cite or link to this item: https://doi.org/10.1002/prot.22994
DC FieldValue
dc.titleA comparison of the dynamics of pantothenate synthetase from M. tuberculosis and E. coli: Computational studies
dc.contributor.authorTan, Y.S.
dc.contributor.authorFuentes, G.
dc.contributor.authorVerma, C.
dc.date.accessioned2014-10-27T08:18:54Z
dc.date.available2014-10-27T08:18:54Z
dc.date.issued2011-06
dc.identifier.citationTan, Y.S., Fuentes, G., Verma, C. (2011-06). A comparison of the dynamics of pantothenate synthetase from M. tuberculosis and E. coli: Computational studies. Proteins: Structure, Function and Bioinformatics 79 (6) : 1715-1727. ScholarBank@NUS Repository. https://doi.org/10.1002/prot.22994
dc.identifier.issn08873585
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/99815
dc.description.abstractPantothenate 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. © 2011 Wiley-Liss, Inc.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1002/prot.22994
dc.sourceScopus
dc.subjectDomain motions
dc.subjectE. coli
dc.subjectGate loop
dc.subjectM. tuberculosis
dc.subjectMolecular dynamics simulations
dc.subjectPantothenate synthetase
dc.typeArticle
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.description.doi10.1002/prot.22994
dc.description.sourcetitleProteins: Structure, Function and Bioinformatics
dc.description.volume79
dc.description.issue6
dc.description.page1715-1727
dc.identifier.isiut000290485500003
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