2bpn

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(New page: 200px<br /><applet load="2bpn" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bpn" /> '''SOLUTION STRUCTURE OF DESULFOVIBRIO VULGARIS...)
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[[Image:2bpn.gif|left|200px]]<br /><applet load="2bpn" size="350" color="white" frame="true" align="right" spinBox="true"
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'''SOLUTION STRUCTURE OF DESULFOVIBRIO VULGARIS (HILDENBOROUGH) FERRICYTOCHROME C3, NMR, 20 STRUCTURES'''<br />
'''SOLUTION STRUCTURE OF DESULFOVIBRIO VULGARIS (HILDENBOROUGH) FERRICYTOCHROME C3, NMR, 20 STRUCTURES'''<br />
==Overview==
==Overview==
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The NMR structure of the oxidised wild-type cytochrome c3 from, Desulfovibrio vulgaris Hildenborough was determined in solution. Using a, newly developed methodology, NMR data from the K45Q mutant was then, grafted onto data from the wild-type protein to determine the structure in, the region of the mutation. The structural origins of the redox-Bohr, effect and haem-haem cooperativities are discussed with respect to the, redox-related conformational changes observed in solution.
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The NMR structure of the oxidised wild-type cytochrome c3 from Desulfovibrio vulgaris Hildenborough was determined in solution. Using a newly developed methodology, NMR data from the K45Q mutant was then grafted onto data from the wild-type protein to determine the structure in the region of the mutation. The structural origins of the redox-Bohr effect and haem-haem cooperativities are discussed with respect to the redox-related conformational changes observed in solution.
==About this Structure==
==About this Structure==
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2BPN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_vulgaris Desulfovibrio vulgaris] with HEC as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BPN OCA].
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2BPN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_vulgaris Desulfovibrio vulgaris] with <scene name='pdbligand=HEC:'>HEC</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BPN OCA].
==Reference==
==Reference==
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[[Category: Desulfovibrio vulgaris]]
[[Category: Desulfovibrio vulgaris]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Aguiar, A.P.]]
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[[Category: Aguiar, A P.]]
[[Category: Brennan, L.]]
[[Category: Brennan, L.]]
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[[Category: Messias, A.C.]]
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[[Category: Messias, A C.]]
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[[Category: Turner, D.L.]]
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[[Category: Turner, D L.]]
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[[Category: Xavier, A.V.]]
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[[Category: Xavier, A V.]]
[[Category: HEC]]
[[Category: HEC]]
[[Category: cytochrome c3]]
[[Category: cytochrome c3]]
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[[Category: transduction]]
[[Category: transduction]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:52:17 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:40:15 2008''

Revision as of 14:40, 21 February 2008


2bpn

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SOLUTION STRUCTURE OF DESULFOVIBRIO VULGARIS (HILDENBOROUGH) FERRICYTOCHROME C3, NMR, 20 STRUCTURES

Overview

The NMR structure of the oxidised wild-type cytochrome c3 from Desulfovibrio vulgaris Hildenborough was determined in solution. Using a newly developed methodology, NMR data from the K45Q mutant was then grafted onto data from the wild-type protein to determine the structure in the region of the mutation. The structural origins of the redox-Bohr effect and haem-haem cooperativities are discussed with respect to the redox-related conformational changes observed in solution.

About this Structure

2BPN is a Single protein structure of sequence from Desulfovibrio vulgaris with as ligand. Full crystallographic information is available from OCA.

Reference

Solution structures of tetrahaem ferricytochrome c3 from Desulfovibrio vulgaris (Hildenborough) and its K45Q mutant: the molecular basis of cooperativity., Messias AC, Aguiar AP, Brennan L, Salgueiro CA, Saraiva LM, Xavier AV, Turner DL, Biochim Biophys Acta. 2006 Feb;1757(2):143-53. Epub 2006 Feb 20. PMID:16527248

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