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1yk4

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(New page: 200px<br /><applet load="1yk4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yk4, resolution 0.69&Aring;" /> '''Ultra-high resolutio...)
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[[Image:1yk4.gif|left|200px]]<br /><applet load="1yk4" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1yk4.gif|left|200px]]<br /><applet load="1yk4" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1yk4, resolution 0.69&Aring;" />
caption="1yk4, resolution 0.69&Aring;" />
'''Ultra-high resolution structure of Pyrococcus abyssi rubredoxin W4L/R5S'''<br />
'''Ultra-high resolution structure of Pyrococcus abyssi rubredoxin W4L/R5S'''<br />
==Overview==
==Overview==
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The crystal structure of Pyrococcus abyssi rubredoxin mutant W4L/R5S was, solved by direct methods. The model of the air-oxidized protein was, refined by partially restrained full-matrix least-squares refinement, against intensity data to 0.69 A resolution. This first, ultrahigh-resolution structure of a rubredoxin provides very detailed and, precise information about the Fe(SCys)(4) centre and its environment, the, peptide-backbone stereochemistry, H atoms and hydrogen bonds, static and, dynamic disorder, the solvent structure and the electron-density, distribution. P. abyssi rubredoxin W4L/R5S is the first of a series of, mutants studied by atomic and ultrahigh-resolution X-ray crystallography, which are expected to contribute to the understanding of, structure-function relationships in iron-sulfur proteins.
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The crystal structure of Pyrococcus abyssi rubredoxin mutant W4L/R5S was solved by direct methods. The model of the air-oxidized protein was refined by partially restrained full-matrix least-squares refinement against intensity data to 0.69 A resolution. This first ultrahigh-resolution structure of a rubredoxin provides very detailed and precise information about the Fe(SCys)(4) centre and its environment, the peptide-backbone stereochemistry, H atoms and hydrogen bonds, static and dynamic disorder, the solvent structure and the electron-density distribution. P. abyssi rubredoxin W4L/R5S is the first of a series of mutants studied by atomic and ultrahigh-resolution X-ray crystallography which are expected to contribute to the understanding of structure-function relationships in iron-sulfur proteins.
==About this Structure==
==About this Structure==
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1YK4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_abyssi Pyrococcus abyssi] with FE as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YK4 OCA].
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1YK4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_abyssi Pyrococcus abyssi] with <scene name='pdbligand=FE:'>FE</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YK4 OCA].
==Reference==
==Reference==
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[[Category: Bonisch, H.]]
[[Category: Bonisch, H.]]
[[Category: Ladenstein, R.]]
[[Category: Ladenstein, R.]]
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[[Category: Schmidt, C.L.]]
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[[Category: Schmidt, C L.]]
[[Category: FE]]
[[Category: FE]]
[[Category: electron transport]]
[[Category: electron transport]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 06:51:19 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:06:15 2008''

Revision as of 14:06, 21 February 2008


1yk4, resolution 0.69Å

Drag the structure with the mouse to rotate

Ultra-high resolution structure of Pyrococcus abyssi rubredoxin W4L/R5S

Overview

The crystal structure of Pyrococcus abyssi rubredoxin mutant W4L/R5S was solved by direct methods. The model of the air-oxidized protein was refined by partially restrained full-matrix least-squares refinement against intensity data to 0.69 A resolution. This first ultrahigh-resolution structure of a rubredoxin provides very detailed and precise information about the Fe(SCys)(4) centre and its environment, the peptide-backbone stereochemistry, H atoms and hydrogen bonds, static and dynamic disorder, the solvent structure and the electron-density distribution. P. abyssi rubredoxin W4L/R5S is the first of a series of mutants studied by atomic and ultrahigh-resolution X-ray crystallography which are expected to contribute to the understanding of structure-function relationships in iron-sulfur proteins.

About this Structure

1YK4 is a Single protein structure of sequence from Pyrococcus abyssi with as ligand. Full crystallographic information is available from OCA.

Reference

Ultrahigh-resolution study on Pyrococcus abyssi rubredoxin. I. 0.69 A X-ray structure of mutant W4L/R5S., Bonisch H, Schmidt CL, Bianco P, Ladenstein R, Acta Crystallogr D Biol Crystallogr. 2005 Jul;61(Pt 7):990-1004. Epub 2005, Jun 24. PMID:15983423

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