期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 110, 期 36, 页码 14664-14669出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1308127110
关键词
membrane potential; protonation; charge-dipole interaction; charge relay
资金
- Ministry of Science and Technology of China 973 Project [2009CB918803, 2011CB910301]
- National Science Foundation of China [31130028, 31225011]
The major facilitator superfamily (MFS) is the largest family of secondary active transporters and is present in all life kingdoms. Detailed structural basis of the substrate transport and energy-coupling mechanisms of these proteins remain to be elucidated. YajR is a putative proton-driven MFS transporter found in many Gram-negative bacteria. Here we report the crystal structure of Escherichia coli YajR at 3.15 angstrom resolution in an outward-facing conformation. In addition to having the 12 canonical transmembrane helices, the YajR structure includes a unique 65-residue C-terminal domain which is independently stable. The structure is unique in illustrating the functional role of sequence motif A. This highly conserved element is seen to stabilize the outward conformation of YajR and suggests a general mechanism for the conformational change between the inward and outward states of the MFS transporters.
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