Theoretical Study of Intermolecular Interactions between Critical Residues of Membrane Protein MraY_AA and Promising Antibiotic Muraymycin D2.

ABSTRACT: Phospho-N-acetylmuramoyl-pentapeptide translocase (MraY_AA) from Aquifex aeolicus is the binding target for the nucleotide antibiotic muraymycin D2 (MD2). MraY_AA in the presence of the MD2 ligand has been crystallized and released, while the interactions between the ligand and active-site residues remain less quantitatively and qualitatively defined. We characterized theoretically the key residues involved in noncovalent interactions with MD2 in the MraY_AA active site. We applied the quantum theory of atoms in molecules and natural bond orbital analyses based on the density functional theory method on the solved crystal structure of MraY with the MD2 to quantitatively estimate the intermolecular interactions. The obtained results revealed the p

SUBMITTER: Malek Zadeh S 

PROVIDER: S-EPMC7495448 | biostudies-literature | 2020 Sep

REPOSITORIES: biostudies-literature