1dwr
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MYOGLOBIN (HORSE HEART) WILD-TYPE COMPLEXED WITH CO
OverviewOverview
Small molecules such as NO, O2, CO or H2 are important biological ligands, that bind to metalloproteins to function crucially in processes such as, signal transduction, respiration and catalysis. A key issue for, understanding the regulation of reaction mechanisms in these systems is, whether ligands gain access to the binding sites through specific channels, and docking sites, or by random diffusion through the protein matrix. A, model system for studying this issue is myoglobin, a simple haem protein., Myoglobin has been studied extensively by spectroscopy, crystallography, computation and theory. It serves as an aid to oxygen diffusion but also, binds carbon monoxide, a byproduct of endogenous haem catabolism., Molecular dynamics simulations, random mutagenesis and flash photolysis, studies indicate that ligand migration occurs through a limited number of, pathways involving docking sites. Here we report the 1.4 A resolution, crystal structure of a ligand-binding intermediate in carbonmonoxy, myoglobin that may have far-reaching implications for understanding the, dynamics of ligand binding and catalysis.
About this StructureAbout this Structure
1DWR is a Single protein structure of sequence from Equus caballus with SO4, HEM and CMO as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Structure of a ligand-binding intermediate in wild-type carbonmonoxy myoglobin., Chu K, Vojtchovsky J, McMahon BH, Sweet RM, Berendzen J, Schlichting I, Nature. 2000 Feb 24;403(6772):921-3. PMID:10706294
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