2eas: Difference between revisions

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[[Image:2eas.gif|left|200px]]
{{Seed}}
[[Image:2eas.png|left|200px]]


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{{STRUCTURE_2eas|  PDB=2eas  |  SCENE=  }}  
{{STRUCTURE_2eas|  PDB=2eas  |  SCENE=  }}  


'''Crystal structure of the SR CA2+-ATPASE with bound CPA'''
===Crystal structure of the SR CA2+-ATPASE with bound CPA===




==Overview==
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Ca(2+)-ATPase of skeletal muscle sarcoplasmic reticulum is an ATP-driven Ca(2+) pump consisting of three cytoplasmic domains and 10 transmembrane helices. In the absence of Ca(2+), the three cytoplasmic domains gather to form a compact headpiece, but the ATPase is unstable without an inhibitor. Here we describe the crystal structures of Ca(2+)-ATPase in the absence of Ca(2+) stabilized with cyclopiazonic acid alone and in combination with other inhibitors. Cyclopiazonic acid is located in the transmembrane region of the protein near the cytoplasmic surface. The binding site partially overlaps with that of 2,5-di-tert-butyl-1,4-dihydroxybenzene but is separate from that of thapsigargin. The overall structure is significantly different from that stabilized with thapsigargin: The cytoplasmic headpiece is more upright, and the transmembrane helices M1-M4 are rearranged. Cyclopiazonic acid primarily alters the position of the M1' helix and thereby M2 and M4 and then M5. Because M5 is integrated into the phosphorylation domain, the whole cytoplasmic headpiece moves. These structural changes show how an event in the transmembrane domain can be transmitted to the cytoplasmic domain despite flexible links between them. They also reveal that Ca(2+)-ATPase has considerable plasticity even when fixed by a transmembrane inhibitor, presumably to accommodate thermal fluctuations.
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{{ABSTRACT_PUBMED_17389383}}


==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Interdomain communication in calcium pump as revealed in the crystal structures with transmembrane inhibitors., Takahashi M, Kondou Y, Toyoshima C, Proc Natl Acad Sci U S A. 2007 Apr 3;104(14):5800-5. Epub 2007 Mar 26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17389383 17389383]
Interdomain communication in calcium pump as revealed in the crystal structures with transmembrane inhibitors., Takahashi M, Kondou Y, Toyoshima C, Proc Natl Acad Sci U S A. 2007 Apr 3;104(14):5800-5. Epub 2007 Mar 26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17389383 17389383]
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:[http://www.ncbi.nlm.nih.gov/pubmed/10864315 10864315]
Structural changes in the calcium pump accompanying the dissociation of calcium., Toyoshima C, Nomura H, Nature. 2002 Aug 8;418(6898):605-11. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12167852 12167852]
Crystal structure of the calcium pump with a bound ATP analogue., Toyoshima C, Mizutani T, Nature. 2004 Jul 29;430(6999):529-35. Epub 2004 Jun 30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15229613 15229613]
Lumenal gating mechanism revealed in calcium pump crystal structures with phosphate analogues., Toyoshima C, Nomura H, Tsuda T, Nature. 2004 Nov 18;432(7015):361-8. Epub 2004 Sep 26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15448704 15448704]
Structural role of countertransport revealed in Ca(2+) pump crystal structure in the absence of Ca(2+)., Obara K, Miyashita N, Xu C, Toyoshima I, Sugita Y, Inesi G, Toyoshima C, Proc Natl Acad Sci U S A. 2005 Oct 11;102(41):14489-96. Epub 2005 Sep 6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16150713 16150713]
[[Category: Calcium-transporting ATPase]]
[[Category: Calcium-transporting ATPase]]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
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[[Category: Membrane protein]]
[[Category: Membrane protein]]
[[Category: P-type atpase]]
[[Category: P-type atpase]]
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