Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
2006-6-7
pubmed:abstractText
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 Ca2+ mediated activation indicate that the crystallized state represents an initial stage of ATP modulated deprotonation of E2, preceding the binding of Ca2+ ions in the membrane from the cytoplasmic side. We propose a mechanism of Ca2+ activation of phosphorylation leading directly from the compact E2-ATP form to the Ca2E1-ATP state. In addition, a role of Glu439 in ATP modulation of other steps of the functional cycle is suggested.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/16710301-10864315, http://linkedlifedata.com/resource/pubmed/commentcorrection/16710301-11585827, http://linkedlifedata.com/resource/pubmed/commentcorrection/16710301-11830654, http://linkedlifedata.com/resource/pubmed/commentcorrection/16710301-12138099, http://linkedlifedata.com/resource/pubmed/commentcorrection/16710301-12167852, http://linkedlifedata.com/resource/pubmed/commentcorrection/16710301-12234183, http://linkedlifedata.com/resource/pubmed/commentcorrection/16710301-12269816, http://linkedlifedata.com/resource/pubmed/commentcorrection/16710301-12649284, http://linkedlifedata.com/resource/pubmed/commentcorrection/16710301-12750373, http://linkedlifedata.com/resource/pubmed/commentcorrection/16710301-12763781, http://linkedlifedata.com/resource/pubmed/commentcorrection/16710301-12837835, http://linkedlifedata.com/resource/pubmed/commentcorrection/16710301-12931192, http://linkedlifedata.com/resource/pubmed/commentcorrection/16710301-12949069, http://linkedlifedata.com/resource/pubmed/commentcorrection/16710301-12975374, http://linkedlifedata.com/resource/pubmed/commentcorrection/16710301-13712164, http://linkedlifedata.com/resource/pubmed/commentcorrection/16710301-1388169, http://linkedlifedata.com/resource/pubmed/commentcorrection/16710301-15150270, http://linkedlifedata.com/resource/pubmed/commentcorrection/16710301-15192230, http://linkedlifedata.com/resource/pubmed/commentcorrection/16710301-15229613, http://linkedlifedata.com/resource/pubmed/commentcorrection/16710301-15262996, http://linkedlifedata.com/resource/pubmed/commentcorrection/16710301-15448704, http://linkedlifedata.com/resource/pubmed/commentcorrection/16710301-15618517, http://linkedlifedata.com/resource/pubmed/commentcorrection/16710301-15937493, http://linkedlifedata.com/resource/pubmed/commentcorrection/16710301-16150713, http://linkedlifedata.com/resource/pubmed/commentcorrection/16710301-16331955, http://linkedlifedata.com/resource/pubmed/commentcorrection/16710301-2025413, http://linkedlifedata.com/resource/pubmed/commentcorrection/16710301-2440883, http://linkedlifedata.com/resource/pubmed/commentcorrection/16710301-2942534, http://linkedlifedata.com/resource/pubmed/commentcorrection/16710301-2948563, http://linkedlifedata.com/resource/pubmed/commentcorrection/16710301-2962996, http://linkedlifedata.com/resource/pubmed/commentcorrection/16710301-2970458, http://linkedlifedata.com/resource/pubmed/commentcorrection/16710301-3155517, http://linkedlifedata.com/resource/pubmed/commentcorrection/16710301-4263199, http://linkedlifedata.com/resource/pubmed/commentcorrection/16710301-6223659, http://linkedlifedata.com/resource/pubmed/commentcorrection/16710301-6235229, http://linkedlifedata.com/resource/pubmed/commentcorrection/16710301-6239651, http://linkedlifedata.com/resource/pubmed/commentcorrection/16710301-6263906, http://linkedlifedata.com/resource/pubmed/commentcorrection/16710301-6320465, http://linkedlifedata.com/resource/pubmed/commentcorrection/16710301-6461647, http://linkedlifedata.com/resource/pubmed/commentcorrection/16710301-7592971, http://linkedlifedata.com/resource/pubmed/commentcorrection/16710301-8496159, http://linkedlifedata.com/resource/pubmed/commentcorrection/16710301-8496160, http://linkedlifedata.com/resource/pubmed/commentcorrection/16710301-8515464, http://linkedlifedata.com/resource/pubmed/commentcorrection/16710301-8634322, http://linkedlifedata.com/resource/pubmed/commentcorrection/16710301-9584613, http://linkedlifedata.com/resource/pubmed/commentcorrection/16710301-9757107
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0261-4189
pubmed:author
pubmed:issnType
Print
pubmed:day
7
pubmed:volume
25
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2305-14
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
Modulatory and catalytic modes of ATP binding by the calcium pump.
pubmed:affiliation
Department of Molecular Biology, Aarhus University, Denmark.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't