Helical Stalk Segments S4 and S5 of the Plasma Membrane H+-ATPase from Saccharomyces cerevisiae Are Optimized to Impact Catalytic Site Environment
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference38 articles.
1. Evolution of Substrate Specificities in the P-Type ATPase Superfamily
2. Organization of P-type ATPases: significance of structural diversity
3. Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution
4. Comparison of H+-ATPase and Ca2+-ATPase suggests that a large conformational change initiates P-type ion pump reaction cycles
5. Three-dimensional map of the plasma membrane H+-ATPase in the open conformation
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1. Structural divergence between the two subgroups of P5 ATPases;Biochimica et Biophysica Acta (BBA) - Bioenergetics;2010-06
2. Use of a Fluorescent Maleimide to Probe Structure-Function Relationships in Stalk Segments 4 and 5 of the Yeast Plasma-Membrane H+-ATPase;Annals of the New York Academy of Sciences;2003-04
3. Molecular Architecture of the Phosphorylation Region of the Yeast Plasma Membrane H+-ATPase;Journal of Biological Chemistry;2003-02
4. Stalk Segment 5 of the Yeast Plasma Membrane H+-ATPase;Journal of Biological Chemistry;2002-10
5. Catalytic Phosphorylation of Na,K-ATPase Drives the Outward Movement of Its Cation-Binding H5−H6 Hairpin;Biochemistry;2002-05-25
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