The ABC of binding-protein-dependent transport in Archaea.
The recent solution of the crystal structure of an entire binding-protein-dependent ABC transporter complex from the archaeon Archaeoglobus fulgidus by Locher and his colleagues marks a milestone in the understanding of the ABC transport mechanism. The structure elegantly demonstrates how the motor ATPase alternately opens and closes the inside and outside pores of the transporter and how the substrate-binding protein delivers its substrate. Binding-protein-dependent sugar ABC transporters in the archaea and in bacteria have an additional feature that could connect ABC transporters to gene regulation and to the control of transport activity by cellular processes.
Lee
Sung-Jae
SJ
Department of Biology, Research Institute for Basic Science, Kyung Hee University, Seoul 130-701, Korea.
Böhm
Alex
A
Krug
Michael
M
Boos
Winfried
W
D018528:ATP-Binding Cassette Transporters / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D000255:Adenosine Triphosphate / Q000378:metabolism; D000595:Amino Acid Sequence; D001105:Archaea / Q000378:metabolism*; D001692:Biological Transport; D019848:Gene Expression Regulation, Archaeal; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary; D021122:Protein Subunits
D018528:ATP-Binding Cassette Transporters; D021122:Protein Subunits; D000255:Adenosine Triphosphate