TY - JOUR
T1 - The long and short of colicin action
T2 - The molecular basis for the biological activity of channel-forming colicins
AU - Gouaux, Eric
N1 - Funding Information:
Support for the author's research on membrane proteins is provided by the NIH and Office of Naval Research. EG would like to thank B Ramachandran for helpful comments on the manuscript. EG is a NSF Young Investigator, a Searle Scholar and an Alfred P Sloan Research Fellow.
PY - 1997
Y1 - 1997
N2 - Channel-forming colicins undergo a remarkable series of conformational gyrations during their voyage from the extracellular milieu to the periplasmic membrane. Crystal structures of the intact colicin la molecule and a channel-forming domain of colicin E1 illuminate relationships between the molecular structure and biological function of these voltage-dependent channel-forming toxins.
AB - Channel-forming colicins undergo a remarkable series of conformational gyrations during their voyage from the extracellular milieu to the periplasmic membrane. Crystal structures of the intact colicin la molecule and a channel-forming domain of colicin E1 illuminate relationships between the molecular structure and biological function of these voltage-dependent channel-forming toxins.
UR - http://www.scopus.com/inward/record.url?scp=0031569404&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0031569404&partnerID=8YFLogxK
U2 - 10.1016/S0969-2126(97)00188-3
DO - 10.1016/S0969-2126(97)00188-3
M3 - Review article
C2 - 9083116
AN - SCOPUS:0031569404
SN - 0969-2126
VL - 5
SP - 313
EP - 317
JO - Structure
JF - Structure
IS - 3
ER -