Ontology highlight
ABSTRACT:
SUBMITTER: Parke CL
PROVIDER: S-EPMC2820811 | biostudies-literature | 2010 Feb
REPOSITORIES: biostudies-literature
The Journal of biological chemistry 20091215 8
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 two-water cluster. We conclude that a proton is shared between the lytic water, positioned for gamma-phosphate attack, and a second water that serves as a general base. To our knowledge, this is the fi ...[more]