2grf
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Crystal structure of Scapharca inaequivalvis HBI, M37V mutant in the absence of ligand
OverviewOverview
Protein allostery provides mechanisms for regulation of biological, function at the molecular level. We present here an investigation of, global, ligand-induced allosteric transition in a protein by time-resolved, x-ray diffraction. The study provides a view of structural changes in, single crystals of Scapharca dimeric hemoglobin as they proceed in real, time, from 5 ns to 80 micros after ligand photodissociation. A tertiary, intermediate structure forms rapidly (<5 ns) as the protein responds to, the presence of an unliganded heme within each R-state protein subunit, with key structural changes observed in the heme groups, neighboring, residues, and interface water molecules. This intermediate lays a, foundation for the concerted tertiary and quaternary structural changes, that occur on a microsecond time scale and are associated with the, transition to a low-affinity T-state structure. Reversal of these changes, shows a considerable lag as a T-like structure persists well after ligand, rebinding, suggesting a slow T-to-R transition.
About this StructureAbout this Structure
2GRF is a Single protein structure of sequence from Scapharca inaequivalvis with HEM as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Allosteric action in real time: time-resolved crystallographic studies of a cooperative dimeric hemoglobin., Knapp JE, Pahl R, Srajer V, Royer WE Jr, Proc Natl Acad Sci U S A. 2006 May 16;103(20):7649-54. Epub 2006 May 9. PMID:16684887
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