6hef

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(New page: ==Room temperature structure of the (SR)Ca2+-ATPase Ca2-E1-CaAMPPCP form== <StructureSection load='6hef' size='340' side='right' caption='6hef, resolution 3.54&Aring;' ...)
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==Room temperature structure of the (SR)Ca2+-ATPase Ca2-E1-CaAMPPCP form==
==Room temperature structure of the (SR)Ca2+-ATPase Ca2-E1-CaAMPPCP form==
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<StructureSection load='6hef' size='340' side='right' caption='[[6hef]], [[Resolution|resolution]] 3.54&Aring;' scene=''>
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<StructureSection load='6hef' size='340' side='right'caption='[[6hef]], [[Resolution|resolution]] 3.54&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6hef]] 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=6HEF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HEF FirstGlance]. <br>
<table><tr><td colspan='2'>[[6hef]] 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=6HEF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HEF FirstGlance]. <br>
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== Function ==
== 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).
[[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).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Neutron macromolecular crystallography (NMX) has the potential to provide the experimental input to address unresolved aspects of transport mechanisms and protonation in membrane proteins. However, despite this clear scientific motivation, the practical challenges of obtaining crystals that are large enough to make NMX feasible have so far been prohibitive. Here, the potential impact on feasibility of a more powerful neutron source is reviewed and a strategy for obtaining larger crystals is formulated, exemplified by the calcium-transporting ATPase SERCA1. The challenges encountered at the various steps in the process from crystal nucleation and growth to crystal mounting are explored, and it is demonstrated that NMX-compatible membrane-protein crystals can indeed be obtained.
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Membrane-protein crystals for neutron diffraction.,Sorensen TLM, Hjorth-Jensen SJ, Oksanen E, Andersen JL, Olesen C, Moller JV, Nissen P Acta Crystallogr D Struct Biol. 2018 Dec 1;74(Pt 12):1208-1218. doi:, 10.1107/S2059798318012561. Epub 2018 Nov 30. PMID:30605135<ref>PMID:30605135</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6hef" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Large Structures]]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
[[Category: Andersen, J L]]
[[Category: Andersen, J L]]

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Room temperature structure of the (SR)Ca2+-ATPase Ca2-E1-CaAMPPCP form

PDB ID 6hef

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