|
|||||
|
|
Insights into the structure of the PmrD protein with molecular dynamics simulations |
|
| Authors: | Vasileios A Tatsis Ioannis G Tsoulos Christos S Krinas Charalampos Alexopoulos Athanassios Stavrakoudis |
| Institution: | aDepartment of Information and Telecommunications Engineering, University of West Macedonia, Kozani, Greece;bDepartment of Communications, Informatics and Management, Technological Educational Institute of Epirus, Arta, Greece;cGeneral Chemical State Laboratory, Tsoha 16, 115 21 Athens, Greece;dDepartment of Economics, University of Ioannina, Panepistimioupoli, GR-451 10 Ioannina, Greece |
| Abstract: | Resistance to cationic antimicrobial peptide polymyxin B from Gram-negative bacteria is accomplished by two-component systems (TCSs), protein complexes PmrA/PmrB and PhoP/PhoQ. PmrD is the first protein identified to mediate the connectivity between two TCSs. The 3D structure of PmrD has been recently solved by NMR and its unique fold was revealed. Here, a molecular dynamics study is presented started from the NMR structure. Numerous hydrophobic and electrostatic interactions were identified to contribute to PmrD's 3D stability. Moreover, the mobility of the five loops that connect the protein's six β-strands has been explored. Solvent-accessible surface area calculation revealed that a Leucine-rich hydrophobic cluster of the protein stabilized the protein's structure. |
| Keywords: | β -Barrel Computer simulation Leucine-rich hydrophobic cluster Molecular dynamics Polymyxin resistance PmrD |
| 本文献已被 ScienceDirect 等数据库收录！ | |