Ontology highlight
ABSTRACT:
SUBMITTER: Jensen AM
PROVIDER: S-EPMC1478189 | biostudies-literature | 2006 Jun
REPOSITORIES: biostudies-literature
Jensen Anne-Marie Lund AM Sørensen Thomas Lykke-Møller TL Olesen Claus C Møller Jesper Vuust JV Nissen Poul P
The EMBO journal 20060518 11
We present crystal structures of the calcium-free E2 state of the sarcoplasmic reticulum Ca2+ -ATPase, stabilized by the inhibitor thapsigargin and the ATP analog AMPPCP. The structures allow us to describe the ATP binding site in a modulatory mode uncoupled from the Asp351 phosphorylation site. The Glu439 side chain interacts with AMPPCP via an Mg2+ ion in accordance with previous Fe2+ -cleavage studies implicating this residue in the ATPase cycle and in magnesium binding. Functional data on Ca ...[more]