4icb

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(New page: 200px<br /><applet load="4icb" size="450" color="white" frame="true" align="right" spinBox="true" caption="4icb, resolution 1.6&Aring;" /> '''PROLINE CIS-TRANS ISO...)
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[[Image:4icb.gif|left|200px]]<br /><applet load="4icb" size="350" color="white" frame="true" align="right" spinBox="true"
caption="4icb, resolution 1.6&Aring;" />
caption="4icb, resolution 1.6&Aring;" />
'''PROLINE CIS-TRANS ISOMERS IN CALBINDIN D9K OBSERVED BY X-RAY CRYSTALLOGRAPHY'''<br />
'''PROLINE CIS-TRANS ISOMERS IN CALBINDIN D9K OBSERVED BY X-RAY CRYSTALLOGRAPHY'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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4ICB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=4ICB OCA].
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4ICB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ICB OCA].
==Reference==
==Reference==
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[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Svensson, L.A.]]
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[[Category: Svensson, L A.]]
[[Category: CA]]
[[Category: CA]]
[[Category: calcium-binding protein]]
[[Category: calcium-binding protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:39:24 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:13:40 2008''

Revision as of 17:13, 21 February 2008


4icb, resolution 1.6Å

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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 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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