Please use this identifier to cite or link to this item:
|Title:||A comparison of the dynamics of pantothenate synthetase from M. tuberculosis and E. coli: Computational studies|
Molecular dynamics simulations
|Citation:||Tan, 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|
|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. © 2011 Wiley-Liss, Inc.|
|Source Title:||Proteins: Structure, Function and Bioinformatics|
|Appears in Collections:||Staff Publications|
Show full item record
Files in This Item:
There are no files associated with this item.
checked on Jul 10, 2018
WEB OF SCIENCETM
checked on May 30, 2018
checked on Jun 29, 2018
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.