Ontology highlight
ABSTRACT:
SUBMITTER: Stone KM
PROVIDER: S-EPMC3552253 | biostudies-literature | 2013 Jan
REPOSITORIES: biostudies-literature
Stone Katherine M KM Voska Jeda J Kinnebrew Maia M Pavlova Anna A Junk Matthias J N MJ Han Songi S
Biophysical journal 20130101 2
Oligomerization has important functional implications for many membrane proteins. However, obtaining structural insight into oligomeric assemblies is challenging, as they are large and resist crystallization. We focus on proteorhodopsin (PR), a protein with seven transmembrane α-helices that was found to assemble to hexamers in densely packed lipid membrane, or detergent-solubilized environments. Yet, the structural organization and the subunit interface of these PR oligomers were unknown. We us ...[more]