1v6p

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(New page: 200px<br /><applet load="1v6p" size="450" color="white" frame="true" align="right" spinBox="true" caption="1v6p, resolution 0.87&Aring;" /> '''Crystal structure of...)
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[[Image:1v6p.jpg|left|200px]]<br /><applet load="1v6p" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1v6p, resolution 0.87&Aring;" />
caption="1v6p, resolution 0.87&Aring;" />
'''Crystal structure of Cobrotoxin'''<br />
'''Crystal structure of Cobrotoxin'''<br />
==Overview==
==Overview==
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By using single wavelength anomalous diffraction phasing based on the, anomalous signal from copper atoms, the crystal structure of atratoxin was, determined at the resolution of 1.5 A and was refined to an ultrahigh, resolution of 0.87 A. The ultrahigh resolution electron density maps, allowed the modeling of 38 amino acid residues in alternate conformations, and the location of 322 of 870 possible hydrogen atoms. To get accurate, information at the atomic level, atratoxin-b (an analog of atratoxin with, reduced toxicity) was also refined to an atomic resolution of 0.92 A. By, the sequence and structural comparison of these two atratoxins, Arg(33), and Arg(36) were identified to be critical to their varied toxicity. The, effect of copper ions on the distribution of hydrogen atoms in atratoxin, was discussed, and the interactions between copper ions and protein, residues were analyzed based on a statistical method, revealing a novel, pentahedral copper-binding motif.
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By using single wavelength anomalous diffraction phasing based on the anomalous signal from copper atoms, the crystal structure of atratoxin was determined at the resolution of 1.5 A and was refined to an ultrahigh resolution of 0.87 A. The ultrahigh resolution electron density maps allowed the modeling of 38 amino acid residues in alternate conformations and the location of 322 of 870 possible hydrogen atoms. To get accurate information at the atomic level, atratoxin-b (an analog of atratoxin with reduced toxicity) was also refined to an atomic resolution of 0.92 A. By the sequence and structural comparison of these two atratoxins, Arg(33) and Arg(36) were identified to be critical to their varied toxicity. The effect of copper ions on the distribution of hydrogen atoms in atratoxin was discussed, and the interactions between copper ions and protein residues were analyzed based on a statistical method, revealing a novel pentahedral copper-binding motif.
==About this Structure==
==About this Structure==
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1V6P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Naja_atra Naja atra] with CU, CL, NA and EOH as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1V6P OCA].
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1V6P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Naja_atra Naja atra] with <scene name='pdbligand=CU:'>CU</scene>, <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=NA:'>NA</scene> and <scene name='pdbligand=EOH:'>EOH</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V6P OCA].
==Reference==
==Reference==
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[[Category: short-chain neurotoxin]]
[[Category: short-chain neurotoxin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 04:29:00 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:32:07 2008''

Revision as of 13:32, 21 February 2008

Image:1v6p.jpg

1v6p, resolution 0.87Å

Drag the structure with the mouse to rotate

Crystal structure of Cobrotoxin

Overview

By using single wavelength anomalous diffraction phasing based on the anomalous signal from copper atoms, the crystal structure of atratoxin was determined at the resolution of 1.5 A and was refined to an ultrahigh resolution of 0.87 A. The ultrahigh resolution electron density maps allowed the modeling of 38 amino acid residues in alternate conformations and the location of 322 of 870 possible hydrogen atoms. To get accurate information at the atomic level, atratoxin-b (an analog of atratoxin with reduced toxicity) was also refined to an atomic resolution of 0.92 A. By the sequence and structural comparison of these two atratoxins, Arg(33) and Arg(36) were identified to be critical to their varied toxicity. The effect of copper ions on the distribution of hydrogen atoms in atratoxin was discussed, and the interactions between copper ions and protein residues were analyzed based on a statistical method, revealing a novel pentahedral copper-binding motif.

About this Structure

1V6P is a Single protein structure of sequence from Naja atra with , , and as ligands. Full crystallographic information is available from OCA.

Reference

The atomic resolution crystal structure of atratoxin determined by single wavelength anomalous diffraction phasing., Lou X, Liu Q, Tu X, Wang J, Teng M, Niu L, Schuller DJ, Huang Q, Hao Q, J Biol Chem. 2004 Sep 10;279(37):39094-104. Epub 2004 Jul 12. PMID:15252034

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