1wad: Difference between revisions

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[[Image:1wad.gif|left|200px]]<br /><applet load="1wad" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1wad.gif|left|200px]]
caption="1wad, resolution 1.8&Aring;" />
 
'''CYTOCHROME C3 WITH 4 HEME GROUPS AND ONE CALCIUM ION'''<br />
{{Structure
|PDB= 1wad |SIZE=350|CAPTION= <scene name='initialview01'>1wad</scene>, resolution 1.8&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=HEM:PROTOPORPHYRIN IX CONTAINING FE'>HEM</scene>
|ACTIVITY=
|GENE=
}}
 
'''CYTOCHROME C3 WITH 4 HEME GROUPS AND ONE CALCIUM ION'''
 


==Overview==
==Overview==
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==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 <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].  
1WAD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_gigas Desulfovibrio gigas]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WAD OCA].  


==Reference==
==Reference==
Cytochrome c3 from Desulfovibrio gigas: crystal structure at 1.8 A resolution and evidence for a specific calcium-binding site., Matias PM, Morais J, Coelho R, Carrondo MA, Wilson K, Dauter Z, Sieker L, Protein Sci. 1996 Jul;5(7):1342-54. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8819167 8819167]
Cytochrome c3 from Desulfovibrio gigas: crystal structure at 1.8 A resolution and evidence for a specific calcium-binding site., Matias PM, Morais J, Coelho R, Carrondo MA, Wilson K, Dauter Z, Sieker L, Protein Sci. 1996 Jul;5(7):1342-54. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8819167 8819167]
[[Category: Desulfovibrio gigas]]
[[Category: Desulfovibrio gigas]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: electron transport]]
[[Category: electron transport]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:42:08 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:54:24 2008''

Revision as of 15:54, 20 March 2008

File:1wad.gif


PDB ID 1wad

Drag the structure with the mouse to rotate
, resolution 1.8Å
Ligands: and
Coordinates: save as pdb, mmCIF, xml



CYTOCHROME C3 WITH 4 HEME GROUPS AND ONE CALCIUM ION


OverviewOverview

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 StructureAbout this Structure

1WAD is a Single protein structure of sequence from Desulfovibrio gigas. Full crystallographic information is available from OCA.

ReferenceReference

Cytochrome c3 from Desulfovibrio gigas: crystal structure at 1.8 A resolution and evidence for a specific calcium-binding site., Matias PM, Morais J, Coelho R, Carrondo MA, Wilson K, Dauter Z, Sieker L, Protein Sci. 1996 Jul;5(7):1342-54. PMID:8819167

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