2zbd
From Proteopedia
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[[Image:2zbd.jpg|left|200px]] | [[Image:2zbd.jpg|left|200px]] | ||
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'''Crystal Structure of the SR Calcium Pump with Bound Aluminium Fluoride, ADP and Calcium''' | '''Crystal Structure of the SR Calcium Pump with Bound Aluminium Fluoride, ADP and Calcium''' | ||
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==About this Structure== | ==About this Structure== | ||
- | 2ZBD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. This structure supersedes the now removed PDB entries | + | 2ZBD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. This structure supersedes the now removed PDB entries and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1wpe 1wpe]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZBD OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Toyoshima, C.]] | [[Category: Toyoshima, C.]] | ||
[[Category: Tsuda, T.]] | [[Category: Tsuda, T.]] | ||
- | [[Category: | + | [[Category: Alternative splicing]] |
- | [[Category: | + | [[Category: Atp-binding]] |
- | [[Category: | + | [[Category: Calcium]] |
- | [[Category: | + | [[Category: Calcium transport]] |
- | [[Category: | + | [[Category: Endoplasmic reticulum]] |
- | [[Category: | + | [[Category: Had fold]] |
- | [[Category: | + | [[Category: Hydrolase]] |
- | [[Category: | + | [[Category: Ion transport]] |
- | [[Category: | + | [[Category: Magnesium]] |
- | [[Category: | + | [[Category: Membrane protein]] |
- | [[Category: | + | [[Category: Metal-binding]] |
- | [[Category: | + | [[Category: Nucleotide-binding]] |
- | [[Category: | + | [[Category: P-type atpase]] |
- | [[Category: | + | [[Category: Phosphorylation]] |
- | [[Category: | + | [[Category: Sarcoplasmic reticulum]] |
- | [[Category: | + | [[Category: Transmembrane]] |
- | [[Category: | + | [[Category: Transport]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 20:06:46 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 17:06, 4 May 2008
Crystal Structure of the SR Calcium Pump with Bound Aluminium Fluoride, ADP and Calcium
Overview
P-type ion transporting ATPases are ATP-powered ion pumps that establish ion concentration gradients across biological membranes. Transfer of bound cations to the lumenal or extracellular side occurs while the ATPase is phosphorylated. Here we report at 2.3 A resolution the structure of the calcium-ATPase of skeletal muscle sarcoplasmic reticulum, a representative P-type ATPase that is crystallized in the absence of Ca2+ but in the presence of magnesium fluoride, a stable phosphate analogue. This and other crystal structures determined previously provide atomic models for all four principal states in the reaction cycle. These structures show that the three cytoplasmic domains rearrange to move six out of ten transmembrane helices, thereby changing the affinity of the Ca2+-binding sites and the gating of the ion pathway. Release of ADP triggers the opening of the lumenal gate and release of phosphate its closure, effected mainly through movement of the A-domain, the actuator of transmembrane gates.
About this Structure
2ZBD is a Single protein structure of sequence from Oryctolagus cuniculus. This structure supersedes the now removed PDB entries and 1wpe. Full crystallographic information is available from OCA.
Reference
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:15448704 Page seeded by OCA on Sun May 4 20:06:46 2008
Categories: Calcium-transporting ATPase | Oryctolagus cuniculus | Single protein | Nomura, H. | Norimatsu, Y. | Ogawa, H. | Toyoshima, C. | Tsuda, T. | Alternative splicing | Atp-binding | Calcium | Calcium transport | Endoplasmic reticulum | Had fold | Hydrolase | Ion transport | Magnesium | Membrane protein | Metal-binding | Nucleotide-binding | P-type atpase | Phosphorylation | Sarcoplasmic reticulum | Transmembrane | Transport