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1su4

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Revision as of 15:08, 11 September 2015

Crystal structure of calcium ATPase with two bound calcium ions

Structural highlights

1su4 is a 1 chain structure with sequence from Oryctolagus cuniculus. This structure supersedes the now removed PDB entry 1eul. The March 2004 RCSB PDB Molecule of the Month feature on The Calcium Pump by David S. Goodsell is 10.2210/rcsb_pdb/mom_2004_3. The October 2009 RCSB PDB Molecule of the Month feature on Sodium-Potassium Pump by David Goodsell is 10.2210/rcsb_pdb/mom_2009_10. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	1iwo, 1vfp
Activity:	Calcium-transporting ATPase, with EC number 3.6.3.8
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

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 PubMed

Calcium ATPase is a member of the P-type ATPases that transport ions across the membrane against a concentration gradient. Here we have solved the crystal structure of the calcium ATPase of skeletal muscle sarcoplasmic reticulum (SERCA1a) at 2.6 A resolution with two calcium ions bound in the transmembrane domain, which comprises ten alpha-helices. The two calcium ions are located side by side and are surrounded by four transmembrane helices, two of which are unwound for efficient coordination geometry. The cytoplasmic region consists of three well separated domains, with the phosphorylation site in the central catalytic domain and the adenosine-binding site on another domain. The phosphorylation domain has the same fold as haloacid dehalogenase. Comparison with a low-resolution electron density map of the enzyme in the absence of calcium and with biochemical data suggests that large domain movements take place during active transport.

Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 A resolution.,Toyoshima C, Nakasako M, Nomura H, Ogawa H Nature. 2000 Jun 8;405(6787):647-55. PMID:10864315^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Toyoshima C, Nakasako M, Nomura H, Ogawa H. Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 A resolution. Nature. 2000 Jun 8;405(6787):647-55. PMID:10864315 doi:http://dx.doi.org/10.1038/35015017

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1su4"

@@ Line 6: / Line 6: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1iwo|1iwo]], [[1vfp|1vfp]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Calcium-transporting_ATPase Calcium-transporting ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.8 3.6.3.8] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1su4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1su4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1su4 RCSB], [http://www.ebi.ac.uk/pdbsum/1su4 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1su4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1su4 OCA], [http://pdbe.org/1su4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1su4 RCSB], [http://www.ebi.ac.uk/pdbsum/1su4 PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 28: / Line 28: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1su4" style="background-color:#fffaf0;"></div>
 ==See Also==

1su4

From Proteopedia

Revision as of 15:08, 11 September 2015

Crystal structure of calcium ATPase with two bound calcium ions

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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