2MTA: Crystal Structure Of A Ternary Electron Transfer Complex Between Methylamine Dehydrogenase, Amicyanin And A C-Type Cytochrome

Citation:
Abstract
The crystal structure of a ternary protein complex has been determined at 2.4 angstrom resolution. The complex is composed of three electron transfer proteins from Paracoccus denitrificans, the quinoprotein methylamine dehydrogenase, the blue copper protein amicyanin, and the cytochrome c551i. The central region of the c551i is folded similarly to several small bacterial c-type cytochromes; there is a 45-residue extension at the amino terminus and a 25-residue extension at the carboxyl terminus. The methylamine dehydrogenase-amicyanin interface is largely hydrophobic, whereas the amicyanin-cytochrome interface is more polar, with several charged groups present on each surface. Analysis of the simplest electron transfer pathways between the redox partners points out the importance of other factors such as energetics in determining the electron transfer rates.
PDB ID: 2MTADownload
MMDB ID: 53852
PDB Deposition Date: 1993/10/26
Updated in MMDB: 2012/11
Experimental Method:
x-ray diffraction
Resolution: 2.4  Å
Source Organism:
Similar Structures:
Biological Unit for 2MTA: octameric; determined by author
Molecular Components in 2MTA
Label Count Molecule
Proteins (8 molecules)
2
Methylamine Dehydrogenase (Heavy Subunit)
Molecule annotation
2
Methylamine Dehydrogenase (Light Subunit)
Molecule annotation
2
Amicyanin
Molecule annotation
2
Cytochrome C551i
Molecule annotation
Chemicals (6 molecules)
1
2
2
2
3
2
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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