6rb2

Structure of the (SR)Ca2+-ATPase mutant E340A in the Ca2-E1-CaAMPPCP form

spinqualitylabelsall models 6rb2, resolution 3.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6rb2 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. Method: X-ray diffraction, Resolution 3.2000113Å Ligands: ACP, CA, K 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 sarco(endo)plasmic reticulum Ca(2+)-ATPase (SERCA) is a P-type ATPase that transports Ca(2+) from the cytosol into the sarco(endo)plasmic reticulum (SR/ER) lumen, driven by ATP. This primary transport activity depends on tight coupling between movements of the transmembrane helices forming the two Ca(2+)-binding sites and the cytosolic headpiece mediating ATP hydrolysis. We have addressed the molecular basis for this intramolecular communication by analyzing the structure and functional properties of the SERCA mutant E340A. The mutated Glu340 residue is strictly conserved among the P-type ATPase family of membrane transporters and is located at a seemingly strategic position at the interface between the phosphorylation domain and the cytosolic ends of 5 of SERCA's 10 transmembrane helices. The mutant displays a marked slowing of the Ca(2+)-binding kinetics, and its crystal structure in the presence of Ca(2+) and ATP analog reveals a rotated headpiece, altered connectivity between the cytosolic domains, and an altered hydrogen bonding pattern around residue 340. Supported by molecular dynamics simulations, we conclude that the E340A mutation causes a stabilization of the Ca(2+) sites in a more occluded state, hence displaying slowed dynamics. This finding underpins a crucial role of Glu340 in interdomain communication between the headpiece and the Ca(2+)-binding transmembrane region. The SERCA residue Glu340 mediates interdomain communication that guides Ca(2+) transport.,Geurts MMG, Clausen JD, Arnou B, Montigny C, Lenoir G, Corey RA, Jaxel C, Moller JV, Nissen P, Andersen JP, le Maire M, Bublitz M Proc Natl Acad Sci U S A. 2020 Nov 23. pii: 2014896117. doi:, 10.1073/pnas.2014896117. PMID:33229570 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also ATPase 3D structures

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