[21] Analysis of two-dimensional crystals of Ca2+-ATPase in sarcoplasmic reticulum
作者： K.A. Taylor , L. Dux , S. Varga , H.P. Ting-Beall , A. Martonosi
DOI: 10.1016/0076-6879(88)57083-0
关键词: Membrane 、 Cytoplasm 、 Negative stain 、 Binding site 、 Enzyme 、 Phosphorylation 、 ATPase 、 Chemistry 、 Endoplasmic reticulum 、 Crystallography
摘要: Publisher Summary This chapter focuses on the analysis of two-dimensional crystals Ca 2+ -ATPase in sarcoplasmic reticulum. The -transport ATPase reticulum (SR) is an intrinsic membrane protein with a molecular weight 109,000. It asymmetrically distributed SR much its mass exposed cytoplasmic surface, where it can be visualized by negative staining form 40-A-diameter surface particles. intramembranous portion revealed freeze-etching as particles about 75 A diameter that are more numerous than luminal fracture face membrane. During ATP-dependent transport, alternates between two distinct conformations, E l and 2 . transport initiated interaction ATP conformation. Phosphorylation enzyme followed conversion from into form. completed release E2 conformation, subsequent hydrolysis phosphoenzyme intermediate. conformation stabilized saturation high-affinity binding site or lanthanides.
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