2MTA

CRYSTAL STRUCTURE OF A TERNARY ELECTRON TRANSFER COMPLEX BETWEEN METHYLAMINE DEHYDROGENASE, AMICYANIN AND A C-TYPE CYTOCHROME

Summary for 2MTA

• Entry DOI: 10.2210/pdb2mta/pdb
• Descriptor: METHYLAMINE DEHYDROGENASE (HEAVY SUBUNIT), METHYLAMINE DEHYDROGENASE (LIGHT SUBUNIT), AMICYANIN, ... (8 entities in total)
• Functional Keywords: electron transport
• Biological source: Paracoccus denitrificans; More
• Cellular location: Periplasm: P29894 P22619 P22364; Periplasm (Potential): P29899
• Total number of polymer chains: 4
• Total formula weight: 83349.19

Authors

Chen, L.,Mathews, F.S. (deposition date: 1993-10-26, release date: 1994-01-31, Last modification date: 2025-03-26)

Primary citation

Chen, L.,Durley, R.C.,Mathews, F.S.,Davidson, V.L.
Structure of an electron transfer complex: methylamine dehydrogenase, amicyanin, and cytochrome c551i.
Science, 264:86-90, 1994

PubMed 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.

PubMed: 8140419

Experimental method

X-RAY DIFFRACTION (2.4 Å)