2bwh
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LAUE STRUCTURE OF A SHORT LIVED STATE OF L29W MYOGLOBIN
OverviewOverview
By using time-resolved x-ray crystallography at room temperature, structural relaxations and ligand migration were examined in myoglobin, (Mb) mutant L29W from nanoseconds to seconds after photodissociation of, carbon monoxide (CO) from the heme iron by nanosecond laser pulses. The, data were analyzed in terms of transient kinetics by fitting trial, functions to integrated difference electron density values obtained from, select structural moieties, thus allowing a quantitative description of, the processes involved. The observed relaxations are linked to other, investigations on protein dynamics. At the earliest times, the heme has, already completely relaxed into its domed deoxy structure, and there is no, photo-dissociated CO visible at the primary docking site. Initial, relaxations of ... [(full description)]
About this StructureAbout this Structure
2BWH is a [Single protein] structure of sequence from [[1]] with HEM and CMO as [ligands]. Full crystallographic information is available from [OCA].
ReferenceReference
Ligand migration pathway and protein dynamics in myoglobin: a time-resolved crystallographic study on L29W MbCO., Schmidt M, Nienhaus K, Pahl R, Krasselt A, Anderson S, Parak F, Nienhaus GU, Srajer V, Proc Natl Acad Sci U S A. 2005 Aug 16;102(33):11704-9. Epub 2005 Aug 5. PMID:16085709
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