1wad: Difference between revisions

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New page: left|200px<br /><applet load="1wad" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wad, resolution 1.8Å" /> '''CYTOCHROME C3 WITH 4 ...
 
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[[Image:1wad.gif|left|200px]]<br /><applet load="1wad" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1wad.gif|left|200px]]<br /><applet load="1wad" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1wad, resolution 1.8&Aring;" />
caption="1wad, resolution 1.8&Aring;" />
'''CYTOCHROME C3 WITH 4 HEME GROUPS AND ONE CALCIUM ION'''<br />
'''CYTOCHROME C3 WITH 4 HEME GROUPS AND ONE CALCIUM ION'''<br />


==Overview==
==Overview==
Crystals of the tetraheme cytochrome c3 from sulfate-reducing bacteria, Desulfovibrio gigas (Dg) (MW 13 kDa, 111 residues, four heme groups) were, obtained and X-ray diffraction data collected to 1.8 A resolution. The, structure was solved by the method of molecular replacement and the, resulting model refined to a conventional R-factor of 14.9%. The, three-dimensional structure shows many similarities to other known crystal, structures of tetraheme c3 cytochromes, but it also shows some remarkable, differences. In particular, the location of the aromatic residues around, the heme groups, which may play a fundamental role in the electron, transfer processes of the molecule, are well conserved in the cases of, hemes I, III, and IV. However, heme II has an aromatic environment that is, completely different to that found in other related cytochromes c3., Another unusual feature is the presence of a Ca2+ ion coordinated by, oxygen atoms supplied by the protein within a loop near the N-terminus. It, is speculated that this loop may be stabilized by the presence of this, Ca2+ ion, may contribute to heme-redox perturbation, and might even be, involved in the specificity of recognition with its redox partner.
Crystals of the tetraheme cytochrome c3 from sulfate-reducing bacteria Desulfovibrio gigas (Dg) (MW 13 kDa, 111 residues, four heme groups) were obtained and X-ray diffraction data collected to 1.8 A resolution. The structure was solved by the method of molecular replacement and the resulting model refined to a conventional R-factor of 14.9%. The three-dimensional structure shows many similarities to other known crystal structures of tetraheme c3 cytochromes, but it also shows some remarkable differences. In particular, the location of the aromatic residues around the heme groups, which may play a fundamental role in the electron transfer processes of the molecule, are well conserved in the cases of hemes I, III, and IV. However, heme II has an aromatic environment that is completely different to that found in other related cytochromes c3. Another unusual feature is the presence of a Ca2+ ion coordinated by oxygen atoms supplied by the protein within a loop near the N-terminus. It is speculated that this loop may be stabilized by the presence of this Ca2+ ion, may contribute to heme-redox perturbation, and might even be involved in the specificity of recognition with its redox partner.


==About this Structure==
==About this Structure==
1WAD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_gigas Desulfovibrio gigas] with CA and HEM as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1WAD OCA].  
1WAD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_gigas Desulfovibrio gigas] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WAD OCA].  


==Reference==
==Reference==
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[[Category: Desulfovibrio gigas]]
[[Category: Desulfovibrio gigas]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Carrondo, M.A.]]
[[Category: Carrondo, M A.]]
[[Category: Coelho, R.]]
[[Category: Coelho, R.]]
[[Category: Dauter, Z.]]
[[Category: Dauter, Z.]]
[[Category: Matias, P.M.]]
[[Category: Matias, P M.]]
[[Category: Morais, J.]]
[[Category: Morais, J.]]
[[Category: Sieker, L.]]
[[Category: Sieker, L.]]
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[[Category: electron transport]]
[[Category: electron transport]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:42:08 2008''