View source for 2dqs

[[Image:2dqs.jpg|left|200px]]

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{{STRUCTURE_2dqs|  PDB=2dqs  |  SCENE=  }} 

'''Crystal structure of the calcium pump with amppcp in the absence of calcium'''


==Overview==
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.

==About this Structure==
2DQS is a [[Single protein]] structure of 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=2DQS OCA]. 

==Reference==
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]
[[Category: Calcium-transporting ATPase]]
[[Category: Oryctolagus cuniculus]]
[[Category: Single protein]]
[[Category: Norimatsu, Y.]]
[[Category: Toyoshima, C.]]
[[Category: Tsueda, J.]]
[[Category: Amppcp]]
[[Category: Hydrolase]]
[[Category: Membrane protein]]
[[Category: P-type atpase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May  7 08:42:26 2008''