TY - JOUR
T1 - Flipping the Switch “On” for Aminoglycoside-Resistance Enzymes
T2 - The Mechanism Is Finally Revealed!
AU - Ngo, Huy X.
AU - Garneau-Tsodikova, Sylvie
N1 - Publisher Copyright:
© 2016 Elsevier Ltd
PY - 2016
Y1 - 2016
N2 - In a recent issue of Structure, Caldwell et al. (2016) determined crystal structures of APH(2″)-Ia in complex with various combinations of aminoglycosides and nucleosides, which compellingly revealed that the catalytic activity of this resistance enzyme is regulated by a conformational change of the triphosphate of GTP, a mechanism previously unknown for antibiotic kinases.
AB - In a recent issue of Structure, Caldwell et al. (2016) determined crystal structures of APH(2″)-Ia in complex with various combinations of aminoglycosides and nucleosides, which compellingly revealed that the catalytic activity of this resistance enzyme is regulated by a conformational change of the triphosphate of GTP, a mechanism previously unknown for antibiotic kinases.
UR - http://www.scopus.com/inward/record.url?scp=84982085427&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84982085427&partnerID=8YFLogxK
U2 - 10.1016/j.str.2016.06.006
DO - 10.1016/j.str.2016.06.006
M3 - Short survey
C2 - 27387794
AN - SCOPUS:84982085427
SN - 0969-2126
VL - 24
SP - 1011
EP - 1013
JO - Structure
JF - Structure
IS - 7
ER -