Flexibility observed in high resolution structures of <Emphasis Type="Italic">Streptomyces aureofaciens</Emphasis> ribonucleases determined by diffraction methods |
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Authors: | Jozef Ševčík |
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Institution: | (1) Department of Chemistry, Technical University of Denmark, Building 207, 2800 Kgs. Lyngby, Denmark;(2) Carlsberg Laboratory, Gamle Carlsberg Vej 10, 1799 Copenhagen V, Denmark; |
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Abstract: | It has been widely accepted to distinguish between static structures determined by diffraction methods and dynamic structures
determined by nuclear magnetic resonance (NMR). The dynamics of NMR structures is demonstrated by an ensemble of a number
of overlaid structures. This cannot be seen in one structure determined by diffraction methods. However, it is possible to
see the flexibility of a protein molecule in a number of structures of the same protein determined by X-ray techniques which
is manifested by different conformations of main-chain. Multiple protein structure determination does not provide identical
structures as a result of various factors including flexibility. Overlap of structures of a protein determined at atomic resolution
with high accuracy shows that the root-mean-square deviations (rmsd) of main-chain atoms exceed several fold the accuracy
of the positional parameters of each structure. Overlap of a number of structures of a protein determined by diffraction methods
shows a similar distribution as that determined by NMR. These observations are demonstrated using high resolution structures
of Streptomyces aureofaciens ribonucleases, their mutants and complexes with ligands. |
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Keywords: | |
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