4icb

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spinqualitylabelsall models 4icb, resolution 1.6Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

PROLINE CIS-TRANS ISOMERS IN CALBINDIN D9K OBSERVED BY X-RAY CRYSTALLOGRAPHY

Overview

In a structure of recombinant bovine calbindin D9k, determined, crystallographically to 1.6 A resolution, a proline in mixed, approximately equally populated, cis and trans conformation is observed., Isomers of this kind have not been reported in structure determinations of, calbindin D9k to 2.3 A resolution or in any other crystallographically, determined protein structure. The cis-trans isomerization occurs at the, peptide bond between Gly42 and Pro43, which is in agreement with results, from two-dimensional 1H nuclear magnetic resonance spectroscopy, experiments on solutions of calbindin D9k. Alternative backbone stretches, have been modeled and refined by stereochemical restrained least-squares, refinement for the segment Lys41 to Pro43. The final R-value was 0.188., The structural perturbations accompanying the cis-trans isomerization are, found to be very localized. The largest positional differences are, observed at residue Gly42, in which the alternative positions of the, oxygen atom are 3.6 A apart.

About this Structure

4ICB is a Single protein structure of sequence from Bos taurus with CA as ligand. Full crystallographic information is available from OCA.

Reference

Proline cis-trans isomers in calbindin D9k observed by X-ray crystallography., Svensson LA, Thulin E, Forsen S, J Mol Biol. 1992 Feb 5;223(3):601-6. PMID:1542107

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