ATP Hydrolysis in Eg5 Kinesin Involves a Catalytic Two-water Mechanism

Motor proteins couple steps in ATP binding and hydrolysis to conformational switching both in and remote from the active site. In our kinesin·AMPPPNP crystal structure, closure of the active site results in structural transformations appropriate for microtubule binding and organizes an orthosteric t...

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Veröffentlicht in:	The Journal of biological chemistry 2010-02, Vol.285 (8), p.5859-5867
Hauptverfasser:	Parke, Courtney L., Wojcik, Edward J., Kim, Sunyoung, Worthylake, David K.
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenylyl Imidodiphosphate - chemistry Adenylyl Imidodiphosphate - metabolism Catalysis Catalytic Domain - physiology Crystallography, X-Ray Enzymes/ATPases Enzymes/Catalysis Enzymes/Mechanisms Enzymes/Structure Enzymology Humans Hydrolysis Kinesins - chemistry Kinesins - genetics Kinesins - metabolism Methods/X-ray Crystallography Molecular Motors Molecular Motors/Kinesin Phosphates - chemistry Phosphates - metabolism Protein Structure, Tertiary - physiology Protein/Conformation Protons Water - chemistry Water - metabolism
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