Ca2+ binding to sarcoplasmic reticulum ATPase revisited. I. Mechanism of affinity and cooperativity modulation by H+ and Mg2+.
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TLDR
The Ca2+ binding curves were analyzed according to a model in which they result from a sequential binding of two Ca2+, each binding step being modified by H+ and Mg2+, to explain the changes in the apparent affinity and cooperativity.About:
This article is published in Journal of Biological Chemistry.The article was published on 1993-05-25 and is currently open access. It has received 73 citations till now. The article focuses on the topics: Cooperativity & Calcium ATPase.read more
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Journal ArticleDOI
Structural organization, ion transport, and energy transduction of p-type atpases
Journal ArticleDOI
Structural role of countertransport revealed in Ca(2+) pump crystal structure in the absence of Ca(2+).
Koji Obara,Naoyuki Miyashita,Cheng Xu,Itaru Toyoshima,Yuji Sugita,Giuseppe Inesi,Chikashi Toyoshima +6 more
TL;DR: Atomic models of the Ca(2+) binding sites with explicit hydrogens derived by continuum electrostatic calculations show how water and protons fill the space and compensate charge imbalance created by Ca( 2+)-release, and suggest that H(+) countertransport is a consequence of a requirement for maintaining structural integrity of the empty Ca (2+)-binding sites.
Journal ArticleDOI
Modulatory and catalytic modes of ATP binding by the calcium pump
TL;DR: A mechanism of Ca2+ activation of phosphorylation leading directly from the compact E2‐ATP form to the Ca2E1‐ATp state is proposed and a role of Glu439 in ATP modulation of other steps of the functional cycle is suggested.
Journal ArticleDOI
Dissection of the functional domains of the sarcoplasmic reticulum Ca2+-ATPase by site-directed mutagenesis
TL;DR: The results of site-directed mutagenesis studies of the sarcoplasmic reticulum Ca2+-ATPase are reviewed, and regions important to the specific inhibition by thapsigargin have been identified by analysis of Ca2-atPase/Na+, K+- ATPase chimeric constructs.
Journal ArticleDOI
Dissection of the functional differences between sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA) 1 and 3 isoforms by steady-state and transient kinetic analyses.
Leonard Dode,Bente Vilsen,Kurt Van Baelen,Frank Wuytack,Johannes D. Clausen,Jens Peter Andersen +5 more
TL;DR: The transient-kinetic analysis traced several of the differences from SERCA1a to an enhancement of the rate of dephosphorylation of the E 2P phosphoenzyme intermediate, which was most pronounced at alkaline pH and increased with the length of the alternatively spliced C terminus.
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