2yfy

SERCA in the HnE2 State Complexed With Debutanoyl Thapsigargin

spinqualitylabelsall models 2yfy, resolution 3.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2yfy is a 1 chain structure with sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 9TN, K, MG Related: 1iwo, 2c9m, 1t5s, 1vfp, 2c88, 1xp5, 2agv, 1wpg, 1su4, 2c8l, 1fqu, 1kju, 1t5t, 2by4, 2c8k, 2voy Activity: Calcium-transporting ATPase, with EC number 3.6.3.8 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [AT2A1_RABIT] This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Contributes to calcium sequestration involved in muscular excitation/contraction (By similarity). Publication Abstract from PubMed The structural elucidation of membrane proteins continues to gather pace, but we know little about their molecular interactions with the lipid environment or how they interact with the surrounding bilayer. Here, with the aid of low-resolution X-ray crystallography, we present direct structural information on membrane interfaces as delineated by lipid phosphate groups surrounding the sarco(endo)plasmic reticulum Ca(2+)-ATPase (SERCA) in its phosphorylated and dephosphorylated Ca(2+)-free forms. The protein-lipid interactions are further analysed using molecular dynamics simulations. We find that SERCA adapts to membranes of different hydrophobic thicknesses by inducing local deformations in the lipid bilayers and by undergoing small rearrangements of the amino-acid side chains and helix tilts. These mutually adaptive interactions allow smooth transitions through large conformational changes associated with the transport cycle of SERCA, a strategy that may be of general nature for many membrane proteins. Mutual adaptation of a membrane protein and its lipid bilayer during conformational changes.,Sonntag Y, Musgaard M, Olesen C, Schiott B, Moller JV, Nissen P, Thogersen L Nat Commun. 2011;2:304. PMID:21556058 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also ATPase 3D structures

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