Crystal structures of a membrane protein transporter in three different conformational states provide insights into the transport mechanism

Beckstein, Oliver

Cameron, Alexander D.

Henderson, Peter J. F.

Iwata, So

Sansom, Mark S. P.

Shimamura, Tatsuro

Weyand, Simone

Journal of Synchrotron Radiation

English

PubMed

Simone Weyand

Tatsuro Shimamura

Oliver Beckstein

Mark S. P. Sansom

So Iwata

Peter J. F. Henderson

Alexander D. Cameron

Crossref

The alternating access mechanism of transport as observed in the sodium-hydantoin transporter Mhp1

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

Weyand, S

Shimamura, T

Beckstein, O

Sansom, MS

Iwata, S

Henderson, PJ

Cameron, AD

Oxford University Research Archive (ORA)

The alternating access mechanism of transport as observed in the sodium-hydantoin transporter Mhp1.

Oxford University Research Archive

Sansom, M. S. P. (Mark S. P.)

Henderson, P. J. F. (Peter J. F.)

Cameron, Alexander

Warwick Research Archives Portal Repository

The alternating access mechanism of transport as observed in the sodium-hydantoin transporter Mhp1

Cellular and Molecular Biology,

Membrane Transport and Metabolism, edited by

http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=3004247

The alternating access mechanism of transport as observed in the sodium-hydantoin transporter Mhp1

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Crossref

Oxford University Research Archive (ORA)

Oxford University Research Archive

Warwick Research Archives Portal Repository