期刊
STRUCTURE
卷 23, 期 2, 页码 290-301出版社
CELL PRESS
DOI: 10.1016/j.str.2014.12.012
关键词
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资金
- Wellcome Trust [092970/Z/10/Z, 102890/Z/13/Z]
- Medical Research Council (MRC) [G0900399]
- Max Planck Society
- NIH, NINDS
- MRC [G0900076/1]
- EPSRC [EP/F068085/1]
- Science Foundation Ireland [07/IN.1/B1836, 12/IA/1255]
- FP7 COST Action [CM0902]
- NIH [P50GM073210, U54GM094599]
- Danish Council for Independent Research in Natural Sciences
- Wellcome Trust Structural Biology DPhil program
- Engineering and Physical Sciences Research Council [EP/L011972/1, EP/J013501/1, EP/D048559/1, EP/F068085/1] Funding Source: researchfish
- Medical Research Council [G0900399, G0900076] Funding Source: researchfish
- Wellcome Trust [102890/Z/13/Z] Funding Source: researchfish
- EPSRC [EP/J013501/1, EP/F068085/1, EP/L011972/1, EP/D048559/1] Funding Source: UKRI
- MRC [G0900399] Funding Source: UKRI
Proton-coupled oligopeptide transporters belong to the major facilitator superfamily (MFS) of membrane transporters. Recent crystal structures suggest the MFS fold facilitates transport through rearrangement of their two six-helix bundles around a central ligand binding site; how this is achieved, however, is poorly understood. Using modeling, molecular dynamics, crystallography, functional assays, and site-directed spin labeling combined with double electron-electron resonance (DEER) spectroscopy, we present a detailed study of the transport dynamics of two bacterial oligopeptide transporters, PepT(So) and PepT(St). Our results identify several salt bridges that stabilize outward-facing conformations and we show that, for all the current structures of MFS transporters, the first two helices of each of the four inverted-topology repeat units form half of either the periplasmic or cytoplasmic gate and that these function cooperatively in a scissor-like motion to control access to the peptide binding site during transport.
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