2ZBF

Calcium pump crystal structure with bound BeF3 and TG in the absence of calcium

Summary for 2ZBF

• Entry DOI: 10.2210/pdb2zbf/pdb
• Related: 1IWO 1SU4 1VFP 1WPG 2AGV 2DQS 2EAR 2EAS 2EAT 2EAU 2ZBD 2ZBE 2ZBG
• Descriptor: Sarcoplasmic/endoplasmic reticulum calcium ATPase 1, MAGNESIUM ION, BERYLLIUM TRIFLUORIDE ION, ... (5 entities in total)
• Functional Keywords: membrane protein, p-type atpase, had fold, atp-binding, calcium transport, endoplasmic reticulum, hydrolase, ion transport, magnesium, metal-binding, nucleotide-binding, phosphorylation, sarcoplasmic reticulum, transmembrane, transport
• Biological source: Oryctolagus cuniculus (rabbit)
• Cellular location: Endoplasmic reticulum membrane; Multi-pass membrane protein: P04191
• Total number of polymer chains: 1
• Total formula weight: 110369.68

Authors

Toyoshima, C.,Ogawa, H.,Norimatsu, Y. (deposition date: 2007-10-20, release date: 2007-12-11, Last modification date: 2024-10-30)

Primary citation

Toyoshima, C.,Norimatsu, Y.,Iwasawa, S.,Tsuda, T.,Ogawa, H.
How processing of aspartylphosphate is coupled to lumenal gating of the ion pathway in the calcium pump
Proc.Natl.Acad.Sci.Usa, 104:19831-19836, 2007

PubMed Abstract: Ca(2+)-ATPase of skeletal muscle sarcoplasmic reticulum is the best-studied member of the P-type or E1/E2 type ion transporting ATPases. It has been crystallized in seven different states that cover nearly the entire reaction cycle. Here we describe the structure of this ATPase complexed with phosphate analogs BeF(3)(-) and AlF(4)(-) in the absence of Ca(2+), which correspond to the E2P ground state and E2 approximately P transition state, respectively. The luminal gate is open with BeF(3)(-) and closed with AlF(4)(-). These and the E1 approximately P.ADP analog crystal structures show that a two-step rotation of the cytoplasmic A-domain opens and closes the luminal gate through the movements of the M1-M4 transmembrane helices. There are several conformational switches coupled to the rotation, and the one in the cytoplasmic part of M2 has critical importance. In the second step of rotation, positioning of one water molecule couples the hydrolysis of aspartylphosphate to closing of the gate.

PubMed: 18077416
DOI: 10.1073/pnas.0709978104

Experimental method

X-RAY DIFFRACTION (2.4 Å)