NDLI: How processing of aspartylphosphate is coupled to lumenal gating of the ion pathway in the calcium pump

Content Provider	PubMed Central
Author	Toyoshima, Chikashi Yoshiyuki, Norimatsu Iwasawa, Shiho Tsuda, Takeo Ogawa, Haruo
Copyright Year	2007
Abstract	Ca2+-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 BeF3 − and AlF4 − in the absence of Ca2+, which correspond to the E2P ground state and E2∼P transition state, respectively. The luminal gate is open with BeF3 − and closed with AlF4 −. These and the E1∼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.
Related Links	http://dx.doi.org/10.1073/pnas.0709978104
Ending Page	19836
Page Count	6
Starting Page	19831
File Format	PDF
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	50
Volume Number	104
Language	English
Publisher	National Academy of Sciences
Publisher Date	2007-12-11
Access Restriction	Open
Rights Holder	National Academy of Sciences
Subject Keyword	General Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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