English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

Structure at 1.5 Å resolution of cytochrome c552 with its flexible linker segment, a membrane-anchored protein from Paracoccus denitrificans

MPS-Authors
/persons/resource/persons137846

Rajendran,  Chitra
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

/persons/resource/persons137648

Ermler,  Ulrich
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

/persons/resource/persons137800

Michel,  Hartmut
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

Locator
There are no locators available
Fulltext (public)
There are no public fulltexts available
Supplementary Material (public)
There is no public supplementary material available
Citation

Rajendran, C., Ermler, U., Ludwig, B., & Michel, H. (2010). Structure at 1.5 Å resolution of cytochrome c552 with its flexible linker segment, a membrane-anchored protein from Paracoccus denitrificans. Acta Crystallographica Section D - Biological Crystallography, D66(7), 850-854.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0024-D699-8
Abstract
Electron transfer (ET) between the large membrane-integral redox complexes in the terminal part of the respiratory chain is mediated either by a soluble c-type cytochrome, as in mitochondria, or by a membrane-anchored cytochrome c, as described for the ET chain of the bacterium Paracoccus denitrificans. Here, the structure of cytochrome c552 from P. denitrificans with the linker segment that attaches the globular domain to the membrane anchor is presented. Cytochrome c552 including the linker segment was crystallized and its structure was determined by molecular replacement. The structural features provide functionally important information. The prediction of the flexibility of the linker region [Berry & Trumpower (1985), J. Biol. Chem. 260, 2458–2467] was confirmed by our crystal structure. The N-terminal region from residues 13 to 31 is characterized by poor electron density, which is compatible with high mobility of this region. This result indicates that this region is highly flexible, which is functionally important for this protein to shuttle electrons between complexes III and IV in the respiratory chain. Zinc present in the crystallization buffer played a key role in the successful crystallization of this protein. It provided rigidity to the long negatively charged flexible loop by coordinating negatively charged residues from two different molecules and by enhancing the crystal contacts.