3ar6: Difference between revisions
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{{STRUCTURE_3ar6| PDB=3ar6 | SCENE= }} | {{STRUCTURE_3ar6| PDB=3ar6 | SCENE= }} | ||
===Calcium pump crystal structure with bound TNP-ADP and TG in the absence of calcium=== | ===Calcium pump crystal structure with bound TNP-ADP and TG in the absence of calcium=== | ||
{{ABSTRACT_PUBMED_21239683}} | |||
==Function== | |||
[[http://www.uniprot.org/uniprot/AT2A1_RABIT 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). | |||
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
<ref group="xtra">PMID:021239683</ref><references group="xtra"/> | <ref group="xtra">PMID:021239683</ref><references group="xtra"/><references/> | ||
[[Category: Calcium-transporting ATPase]] | [[Category: Calcium-transporting ATPase]] | ||
[[Category: Oryctolagus cuniculus]] | [[Category: Oryctolagus cuniculus]] | ||
Revision as of 11:44, 30 October 2013
Calcium pump crystal structure with bound TNP-ADP and TG in the absence of calciumCalcium pump crystal structure with bound TNP-ADP and TG in the absence of calcium
Template:ABSTRACT PUBMED 21239683
FunctionFunction
[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).
About this StructureAbout this Structure
3ar6 is a 1 chain structure with sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA.
See AlsoSee Also
ReferenceReference
- ↑ Toyoshima C, Yonekura SI, Tsueda J, Iwasawa S. Trinitrophenyl derivatives bind differently from parent adenine nucleotides to Ca2+-ATPase in the absence of Ca2+ Proc Natl Acad Sci U S A. 2011 Jan 14. PMID:21239683 doi:10.1073/pnas.1017659108