id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-308480-t2vukbwp	Liang, Zhongjie	Molecular Basis of NDM-1, a New Antibiotic Resistance Determinant	2011-08-24		.txt	text/plain	4279	206	48	In addition, the detailed analysis indicates that the more flexible and hydrophobic loop1, together with the evolution of more positive-charged loop2 leads to NDM-1 positive strain more potent and extensive in antibiotics resistance compared with other MBLs. Furthermore, through biological experiments, we revealed the molecular basis for antibiotics catalysis of NDM-1 on the enzymatic level. Taking two typical antibiotics, imipenem and carbapenem as example, the docked complex structures revealed that although the antibiotics adopted diverse conformations in the active site, the lactam motifs were positioned in the same orientation by coordinating with zinc ions tightly ( Figure 2C ), which suggested that the catalytic mechanisms were highly conserved among B1 subclass enzymes, as shown in Figure 3 . To gain the structural insight into the mechanism of the potent hydrolysis of NDM-1, the intermolecular interactions of three models of NDM-1, VIM-2 and FEZ-1 in complex with antibiotics meropenem were compared and analyzed in details ( Figure 4A -C).	./cache/cord-308480-t2vukbwp.txt	./txt/cord-308480-t2vukbwp.txt