1hh5

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[[Image:1hh5.jpg|left|200px]]
[[Image:1hh5.jpg|left|200px]]
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{{Structure
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|PDB= 1hh5 |SIZE=350|CAPTION= <scene name='initialview01'>1hh5</scene>, resolution 1.90&Aring;
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The line below this paragraph, containing "STRUCTURE_1hh5", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=HC1:Hec+Binding+Site+For+Residue+A69'>HC1</scene>, <scene name='pdbsite=HC2:Hec+Binding+Site+For+Residue+A70'>HC2</scene> and <scene name='pdbsite=HC3:Hec+Binding+Site+For+Residue+A71'>HC3</scene>
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|LIGAND= <scene name='pdbligand=HEC:HEME+C'>HEC</scene>
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{{STRUCTURE_1hh5| PDB=1hh5 | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hh5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hh5 OCA], [http://www.ebi.ac.uk/pdbsum/1hh5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hh5 RCSB]</span>
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'''CYTOCHROME C7 FROM DESULFUROMONAS ACETOXIDANS'''
'''CYTOCHROME C7 FROM DESULFUROMONAS ACETOXIDANS'''
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[[Category: Haser, R.]]
[[Category: Haser, R.]]
[[Category: Shepard, W.]]
[[Category: Shepard, W.]]
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[[Category: electron transport]]
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[[Category: Electron transport]]
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[[Category: multiheme cytochrome]]
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[[Category: Multiheme cytochrome]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:50:35 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:04:52 2008''
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Revision as of 15:50, 2 May 2008

Template:STRUCTURE 1hh5

CYTOCHROME C7 FROM DESULFUROMONAS ACETOXIDANS


Overview

Multihaem cytochromes play a key role in electron-transport reactions in the periplasm of sulfate- and sulfur-reducing bacteria. The redox proteins grouped in the c3 superfamily also display metal-reducing activities, which make them interesting biotechnological tools. The crystal structure of the fully oxidized cytochrome c7 from Desulfuromonas acetoxidans has been solved by combined molecular-replacement and MAD methods. The structure has been refined at 1.9 A resolution to an R value of 19.1% (R(free) = 24.3%) and includes three haems and 116 water molecules. The protein displays the cytochrome c3 fold in a highly minimized form, while haem 2 and the surrounding protein environment are missing. The geometry of haem packing and of the haem axial ligands and propionates are described and compared with that of c3 cytochromes. The crystal structure is compared with the solution structure recently obtained by NMR methods and with its homologue cytochromes of the c3 superfamily. Comparison of the high number of available structures makes it possible to analyze the structural role of the few highly conserved residues, in addition to the cysteines and histidines that link the porphyrin rings and the Fe atoms to the protein chain.

About this Structure

1HH5 is a Single protein structure of sequence from Desulfuromonas acetoxidans. Full crystallographic information is available from OCA.

Reference

Structure of cytochrome c7 from Desulfuromonas acetoxidans at 1.9 A resolution., Czjzek M, Arnoux P, Haser R, Shepard W, Acta Crystallogr D Biol Crystallogr. 2001 May;57(Pt 5):670-8. Epub 2001, Apr 24. PMID:11320307 Page seeded by OCA on Fri May 2 18:50:35 2008

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