Ontology highlight
ABSTRACT:
SUBMITTER: Fischer G
PROVIDER: S-EPMC2688079 | biostudies-literature | 2009 Jun
REPOSITORIES: biostudies-literature
Fischer Gerhard G Kosinska-Eriksson Urszula U Aponte-Santamaría Camilo C Palmgren Madelene M Geijer Cecilia C Hedfalk Kristina K Hohmann Stefan S de Groot Bert L BL Neutze Richard R Lindkvist-Petersson Karin K
PLoS biology 20090616 6
Aquaporins are transmembrane proteins that facilitate the flow of water through cellular membranes. An unusual characteristic of yeast aquaporins is that they frequently contain an extended N terminus of unknown function. Here we present the X-ray structure of the yeast aquaporin Aqy1 from Pichia pastoris at 1.15 A resolution. Our crystal structure reveals that the water channel is closed by the N terminus, which arranges as a tightly wound helical bundle, with Tyr31 forming H-bond interactions ...[more]