1ymc

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(New page: 200px<br /><applet load="1ymc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ymc, resolution 2.0&Aring;" /> '''THREE-DIMENSIONAL STR...)
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[[Image:1ymc.jpg|left|200px]]<br /><applet load="1ymc" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ymc.jpg|left|200px]]<br /><applet load="1ymc" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1ymc, resolution 2.0&Aring;" />
caption="1ymc, resolution 2.0&Aring;" />
'''THREE-DIMENSIONAL STRUCTURE OF CYANOMET-SULFMYOGLOBIN C'''<br />
'''THREE-DIMENSIONAL STRUCTURE OF CYANOMET-SULFMYOGLOBIN C'''<br />
==Overview==
==Overview==
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The atomic structure of horse heart cyanomet-sulfmyoglobin C has been, established by x-ray crystallographic techniques to a resolution of 2.0 A, with an R value of 0.129. The protoheme IX prosthetic group of this, thermodynamically stable sulfmyoglobin derivative has been converted to a, chlorin in which the pyrrole ring bearing the 4-vinyl group is saturated, and possesses an exocyclic thiolene ring. This study provides the, three-dimensional structure of a protein with an iron-chlorin prosthetic, group. The overall conformation of the surrounding polypeptide chain of, the modified protein is very similar to that of the native protein., However, the addition of the sulfur atom has caused a distortion of the, prosthetic group from that in the native protein to result in the, repositioning of the side chains of some residues in the heme pocket.
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The atomic structure of horse heart cyanomet-sulfmyoglobin C has been established by x-ray crystallographic techniques to a resolution of 2.0 A with an R value of 0.129. The protoheme IX prosthetic group of this thermodynamically stable sulfmyoglobin derivative has been converted to a chlorin in which the pyrrole ring bearing the 4-vinyl group is saturated and possesses an exocyclic thiolene ring. This study provides the three-dimensional structure of a protein with an iron-chlorin prosthetic group. The overall conformation of the surrounding polypeptide chain of the modified protein is very similar to that of the native protein. However, the addition of the sulfur atom has caused a distortion of the prosthetic group from that in the native protein to result in the repositioning of the side chains of some residues in the heme pocket.
==About this Structure==
==About this Structure==
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1YMC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus] with SO4, CYN and CLN as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YMC OCA].
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1YMC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=CYN:'>CYN</scene> and <scene name='pdbligand=CLN:'>CLN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YMC OCA].
==Reference==
==Reference==
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[[Category: Equus caballus]]
[[Category: Equus caballus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Brayer, G.D.]]
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[[Category: Brayer, G D.]]
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[[Category: Evans, S.V.]]
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[[Category: Evans, S V.]]
[[Category: CLN]]
[[Category: CLN]]
[[Category: CYN]]
[[Category: CYN]]
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[[Category: oxygen transport]]
[[Category: oxygen transport]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 06:54:31 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:06:50 2008''

Revision as of 14:06, 21 February 2008

Image:1ymc.jpg

1ymc, resolution 2.0Å

Drag the structure with the mouse to rotate

THREE-DIMENSIONAL STRUCTURE OF CYANOMET-SULFMYOGLOBIN C

Overview

The atomic structure of horse heart cyanomet-sulfmyoglobin C has been established by x-ray crystallographic techniques to a resolution of 2.0 A with an R value of 0.129. The protoheme IX prosthetic group of this thermodynamically stable sulfmyoglobin derivative has been converted to a chlorin in which the pyrrole ring bearing the 4-vinyl group is saturated and possesses an exocyclic thiolene ring. This study provides the three-dimensional structure of a protein with an iron-chlorin prosthetic group. The overall conformation of the surrounding polypeptide chain of the modified protein is very similar to that of the native protein. However, the addition of the sulfur atom has caused a distortion of the prosthetic group from that in the native protein to result in the repositioning of the side chains of some residues in the heme pocket.

About this Structure

1YMC is a Single protein structure of sequence from Equus caballus with , and as ligands. Full crystallographic information is available from OCA.

Reference

Three-dimensional structure of cyanomet-sulfmyoglobin C., Evans SV, Sishta BP, Mauk AG, Brayer GD, Proc Natl Acad Sci U S A. 1994 May 24;91(11):4723-6. PMID:8197124

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