Assembly of a tyr122 hydrophobic cluster in sarcoplasmic reticulum ca2+-atpase synchronizes ca2+ affinity reduction and release with phosphoenzyme isomerization*

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• who: Kazuo Yamasaki from the Kazuo Yamasaki1, Takashi Daiho, Stefania Danko, and Hiroshi Suzuki From the Department of Biochemistry, Asahikawa Medical University, Midorigaoka-Higashi, Asahikawa, Japan Background: Ca2⫹ transport by Ca2⫹-ATPase includes phosphoenzyme isomerization with luminal Ca2⫹ releaseResults: Mutation of Leu119, Tyr122, or Ile, in an interdomain hydrophobic cluster retards release relative to isomerization. Conclusions: There is a transient Ca2⫹-bound state and affinity reduction during release governed by cluster assembly. Significance: Ca2⫹ release is a multistep process directed by head domain gathering on transmembrane helix, . The mechanism whereby events in and around the catalytic site . . .
  

   

  

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