19hc
From Proteopedia
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|PDB= 19hc |SIZE=350|CAPTION= <scene name='initialview01'>19hc</scene>, resolution 1.80Å | |PDB= 19hc |SIZE=350|CAPTION= <scene name='initialview01'>19hc</scene>, resolution 1.80Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene> | + | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=19hc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=19hc OCA], [http://www.ebi.ac.uk/pdbsum/19hc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=19hc RCSB]</span> | ||
}} | }} | ||
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[[Category: Sieker, L.]] | [[Category: Sieker, L.]] | ||
[[Category: Thompson, A W.]] | [[Category: Thompson, A W.]] | ||
| - | [[Category: ACT]] | ||
| - | [[Category: HEM]] | ||
[[Category: cytochrome]] | [[Category: cytochrome]] | ||
[[Category: electron transfer]] | [[Category: electron transfer]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:30:09 2008'' |
Revision as of 15:30, 30 March 2008
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| , resolution 1.80Å | |||||||
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| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
NINE-HAEM CYTOCHROME C FROM DESULFOVIBRIO DESULFURICANS ATCC 27774
Overview
BACKGROUND: Haem-containing proteins are directly involved in electron transfer as well as in enzymatic functions. The nine-haem cytochrome c (9Hcc), previously described as having 12 haem groups, was isolated from cells of Desulfovibrio desulfuricans ATCC 27774, grown under both nitrate- and sulphate-respiring conditions. RESULTS: Models for the primary and three-dimensional structures of this cytochrome, containing 292 amino acid residues and nine haem groups, were derived using the multiple wavelength anomalous dispersion phasing method and refined using 1.8 A diffraction data to an R value of 17.0%. The nine haem groups are arranged into two tetrahaem clusters, with Fe-Fe distances and local protein fold similar to tetrahaem cytochromes c3, while the extra haem is located asymmetrically between the two clusters. CONCLUSIONS: This is the first known three-dimensional structure in which multiple copies of a tetrahaem cytochrome c3-like fold are present in the same polypeptide chain. Sequence homology was found between this cytochrome and the C-terminal region (residues 229-514) of the high molecular weight cytochrome c from Desulfovibrio vulgaris Hildenborough (DvH Hmc). A new haem arrangement in domains III and IV of DvH Hmc is proposed. Kinetic experiments showed that 9Hcc can be reduced by the [NiFe] hydrogenase from D. desulfuricans ATCC 27774, but that this reduction is faster in the presence of tetrahaem cytochrome c3. As Hmc has never been found in D. desulfuricans ATCC 27774, we propose that 9Hcc replaces it in this organism and is therefore probably involved in electron transfer across the membrane.
About this Structure
19HC is a Single protein structure of sequence from Desulfovibrio desulfuricans. Full crystallographic information is available from OCA.
Reference
The primary and three-dimensional structures of a nine-haem cytochrome c from Desulfovibrio desulfuricans ATCC 27774 reveal a new member of the Hmc family., Matias PM, Coelho R, Pereira IA, Coelho AV, Thompson AW, Sieker LC, Gall JL, Carrondo MA, Structure. 1999 Feb 15;7(2):119-30. PMID:10368280
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