3ba6: Difference between revisions
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==Structure of the Ca2E1P phosphoenzyme intermediate of the SERCA Ca2+-ATPase== | ==Structure of the Ca2E1P phosphoenzyme intermediate of the SERCA Ca2+-ATPase== | ||
<StructureSection load='3ba6' size='340' side='right' caption='[[3ba6]], [[Resolution|resolution]] 2.80Å' scene=''> | <StructureSection load='3ba6' size='340' side='right'caption='[[3ba6]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3ba6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BA6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3BA6 FirstGlance]. <br> | <table><tr><td colspan='2'>[[3ba6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BA6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3BA6 FirstGlance]. <br> | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ba/3ba6_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ba/3ba6_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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</div> | </div> | ||
<div class="pdbe-citations 3ba6" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 3ba6" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[ATPase 3D structures|ATPase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Calcium-transporting ATPase]] | [[Category: Calcium-transporting ATPase]] | ||
[[Category: Large Structures]] | |||
[[Category: Oryctolagus cuniculus]] | [[Category: Oryctolagus cuniculus]] | ||
[[Category: Gyrup, C]] | [[Category: Gyrup, C]] | ||
Revision as of 10:39, 31 July 2019
Structure of the Ca2E1P phosphoenzyme intermediate of the SERCA Ca2+-ATPaseStructure of the Ca2E1P phosphoenzyme intermediate of the SERCA Ca2+-ATPase
Structural highlights
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). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe sarcoplasmic reticulum Ca2+-ATPase, a P-type ATPase, has a critical role in muscle function and metabolism. Here we present functional studies and three new crystal structures of the rabbit skeletal muscle Ca2+-ATPase, representing the phosphoenzyme intermediates associated with Ca2+ binding, Ca2+ translocation and dephosphorylation, that are based on complexes with a functional ATP analogue, beryllium fluoride and aluminium fluoride, respectively. The structures complete the cycle of nucleotide binding and cation transport of Ca2+-ATPase. Phosphorylation of the enzyme triggers the onset of a conformational change that leads to the opening of a luminal exit pathway defined by the transmembrane segments M1 through M6, which represent the canonical membrane domain of P-type pumps. Ca2+ release is promoted by translocation of the M4 helix, exposing Glu 309, Glu 771 and Asn 796 to the lumen. The mechanism explains how P-type ATPases are able to form the steep electrochemical gradients required for key functions in eukaryotic cells. The structural basis of calcium transport by the calcium pump.,Olesen C, Picard M, Winther AM, Gyrup C, Morth JP, Oxvig C, Moller JV, Nissen P Nature. 2007 Dec 13;450(7172):1036-42. PMID:18075584[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Calcium-transporting ATPase
- Large Structures
- Oryctolagus cuniculus
- Gyrup, C
- Moller, J V
- Morth, J P
- Nissen, P
- Olesen, C
- Oxvig, C
- Picard, M
- Winther, A M.L
- Alternative splicing
- Aspartyl-phosphoanhydride
- Atp-binding
- Calcium
- Calcium transport
- Endoplasmic reticulum
- Hydrolase
- Ion transport
- Magnesium
- Membrane protein
- Metal-binding
- Nucleotide-binding
- P-type atpase
- Phosphoenzyme
- Phosphorylation
- Sarcoplasmic reticulum
- Transmembrane
- Transport