Repositioning of transmembrane alpha-helices during membrane protein folding
2010 (English)In: Journal of Molecular Biology, ISSN 0022-2836, E-ISSN 1089-8638, Vol. 397, no 1, 190-201 p.Article in journal (Refereed) Published
We have determined the optimal placement of individual transmembrane helices in the Pyrococcus horikoshii Glt(Ph) glutamate transporter homolog in the membrane. The results are in close agreement with theoretical predictions based on hydrophobicity, but do not, in general, match the known three-dimensional structure, suggesting that transmembrane helices can be repositioned relative to the membrane during folding and oligomerization. Theoretical analysis of a database of membrane protein structures provides additional support for this idea. These observations raise new challenges for the structure prediction of membrane proteins and suggest that the classical two-stage model often used to describe membrane protein folding needs to be modified.
Place, publisher, year, edition, pages
2010. Vol. 397, no 1, 190-201 p.
membrane protein; GltPh; protein folding; membrane insertion
Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)
Research subject Biochemistry
IdentifiersURN: urn:nbn:se:su:diva-42790DOI: 10.1016/j.jmb.2010.01.042ISI: 000275785600013PubMedID: 20109468OAI: oai:DiVA.org:su-42790DiVA: diva2:351449