期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 109, 期 1, 页码 107-112出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1109213108
关键词
allostery; cooperativity; structural dynamics; time-resolved crystallography
资金
- US Department of Energy, Basic Energy Sciences, Office of Science [DE-AC02-06CH11357]
- National Institutes of Health (NIH), National Center for Research Resources [RR007707]
- NIH/National Institute of Diabetes and Digestive and Kidney Diseases
Here we present a meta-analysis of a large collection of static structures of a protein in the Protein Data Bank in order to extract the progression of structural events during protein function. We apply this strategy to the homodimeric hemoglobin HbI from Scapharca inaequivalvis. We derive a simple dynamic model describing how binding of the first ligand in one of the two chemically identical subunits facilitates a second binding event in the other partner subunit. The results of our ultrafast time-resolved crystallographic studies support this model. We demonstrate that HbI functions like a homodimeric mechanical device, such as pliers or scissors. Ligand-induced motion originating in one subunit is transmitted to the other via conserved pivot points, where the E and F' helices from two partner subunits are bolted together to form a stable dimer interface permitting slight relative rotation but preventing sliding.
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