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Alternating Access in Maltose Transporter Mediated by Rigid-Body Rotations
Open accessAbstract
ATP-binding cassette transporters couple ATP hydrolysis to substrate translocation through an alternating access mechanism, but the nature of the conformational changes in a transport cycle remains elusive. Previously we reported the structure of the maltose transporter MalFGK2 in an outward-facing conformation where the transmembrane (TM) helices outline a substrate-binding pocket open towards the periplasmic surface and ATP is poised for hydrolysis along the closed nucleotide-binding dimer interface. Here we report the structure of the nucleotide-free maltose transporter in which the substrate binding pocket is only accessible from the cytoplasm and the nucleotide-binding interface is open. Comparison of the same transporter crystallized in two different conformations reveals that alternating access involves rigid-body rotations of the TM subdomains that are coupled to the closure and opening of the nucleotide-binding domain interface. The comparison also reveals that point mutations enabling binding-protein independent transport line dynamic interfaces in the TM region.
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Cites
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Emsley, P., & Cowtan, K. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444904019158 · Cited by 30,571
Smith, P. C., Karpowich, N., Millen, L., Moody, J. E., Rosen, J., Thomas, P. J., & Hunt, J. F. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00576-2 · Cited by 773
Cited by
Chen, L.-Q., Cheung, L. S., Feng, L., Tanner, W., & Frommer, W. B. (2015) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060614-033904 · Cited by 507
Crystal structure of the multidrug transporter P-glycoprotein from Caenorhabditis elegans
Jin, M. S., Oldham, M. L., Zhang, Q., & Chen, J. (2012) · Nature · doi:10.1038/nature11448 · Cited by 465
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ter Beek, J., Guskov, A., & Slotboom, D. J. (2014) · Journal of General Physiology · doi:10.1085/jgp.201411164 · Cited by 384
RCSB Protein Data Bank: Enabling biomedical research and drug discovery
Goodsell, D. S., Zardecki, C., Di Costanzo, L., Duarte, J. M., Hudson, B. P., Persikova, I., Segura, J., Shao, C., Voigt, M., Westbrook, J. D., et al. (2020) · Protein Science · doi:10.1002/pro.3730 · Cited by 353
Refined structures of mouse P‐glycoprotein
Li, J., Jaimes, K. F., & Aller, S. G. (2014) · Protein Science · doi:10.1002/pro.2387 · Cited by 344
Metadata
- Authors
- Khare, D., Oldham, M. L., Orelle, C., Davidson, A. L., & Chen, J.
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2009-02
- Volume
- 33
- Issue
- 4
- Pages
- 528-536
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W2056082671
- Cited by
- 242
- References
- 2
- FWCI
- 11.64
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Khare, D., Oldham, M. L., Orelle, C., Davidson, A. L., & Chen, J. (2009). Alternating Access in Maltose Transporter Mediated by Rigid-Body Rotations. Molecular Cell. https://doi.org/10.1016/j.molcel.2009.01.035
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