2w2e

1.15 Angstrom crystal structure of P.pastoris aquaporin, Aqy1, in a closed conformation at pH 3.5

spinqualitylabelsall models 2w2e, resolution 1.15Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2w2e is a 1 chain structure with sequence from Komagataella pastoris. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BOG, CL Related: 2w1p Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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 to a water molecule within the pore and thereby occluding the channel entrance. Nevertheless, functional assays show that Aqy1 has appreciable water transport activity that aids survival during rapid freezing of P. pastoris. These findings establish that Aqy1 is a gated water channel. Mutational studies in combination with molecular dynamics simulations imply that gating may be regulated by a combination of phosphorylation and mechanosensitivity. Crystal structure of a yeast aquaporin at 1.15 angstrom reveals a novel gating mechanism.,Fischer G, Kosinska-Eriksson U, Aponte-Santamaria C, Palmgren M, Geijer C, Hedfalk K, Hohmann S, de Groot BL, Neutze R, Lindkvist-Petersson K PLoS Biol. 2009 Jun;7(6):e1000130. Epub 2009 Jun 16. PMID:19529756 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Aquaporin

Proteopedia Page Contributors and Editors (what is this?)

OCA