Journal
JOURNAL OF SYNCHROTRON RADIATION
Volume 18, Issue -, Pages 20-23Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S0909049510032449
Keywords
membrane transport; transport protein; alternating access; hydantoins
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Funding
- BBSRC [BB/H000267/1, BB/I019855/1, BB/G023425/1, BB/G020043/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/G023425/1, BEP17032, BB/C51725, B19456, BB/I019855/1, BBS/B/16011, BB/C51725X/1, BB/G020043/1, BB/H000267/1] Funding Source: Medline
- Wellcome Trust Funding Source: Medline
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Secondary active transporters move molecules across cell membranes by coupling this process to the energetically favourable downhill movement of ions or protons along an electrochemical gradient. They function by the alternating access model of transport in which, through conformational changes, the substrate binding site alternately faces either side of the membrane. Owing to the difficulties in obtaining the crystal structure of a single transporter in different conformational states, relatively little structural information is known to explain how this process occurs. Here, the structure of the sodium-benzylhydantoin transporter, Mhp1, from Microbacterium liquefaciens, has been determined in three conformational states; from this a mechanism is proposed for switching from the outward-facing open conformation through an occluded structure to the inward-facing open state.
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