The use of pseudocontact shifts to refine solution structures of paramagnetic metalloproteins: Met80Ala cyano-cytochrome c as an example |
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| Authors: | L Banci I Bertini K L Bren M A Cremonini H B Gray C Luchinat P Turano |
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| Institution: | (1) Department of Chemistry, University of Florence, Via G. Capponi 7, I-50121 Florence, Italy, IT;(2) Arthur Amos Noyes Laboratory, California Institute of Technology, Pasadena, CA 91125, USA, US;(3) Institute of Agricultural Chemistry, University of Bologna, Viale Berti Pichat 10, I-40127 Bologna, Italy, IT |
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| Abstract: | The availability of NOE constraints and of the relative solution structure of a paramagnetic protein permits the use of pseudocontact
shifts as further structural constraints. We have developed a strategy based on: (1) determination of the χ tensor anisotropy
parameters from the starting structure; (2) recalculation of a new structure by using NOE and pseudocontact shift constraints simultaneously; (3) redetermination of the χ tensor anisotropy parameters from the new structure,
and so on until self-consistency. The system investigated is the cyanide derivative of a variant of the oxidized Saccharomyces cerevisiae iso-1-cytochrome c containing the Met80Ala mutation. The structure has been substantially refined. It is shown that the analysis of the deviation
of the experimental pseudocontact shifts from those calculated using the starting structure may be unsound, as may the simple
structure refinement based on the pseudocontact shift constraints only.
Received: 11 July 1995 / Accepted: 30 October 1995 |
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| Keywords: | Solution structure Paramagnetic biomolecules NMR Cytochrome c |
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