2gc4
Structural comparison of the oxidized ternary electron transfer complex of methylamine dehydrogenase, amicyanin and cytochrome c551i from Paracoccus denitrificans with the substrate-reduced, copper free complex at 1.9 A resolution.
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OverviewOverview
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.
About this StructureAbout this Structure
2GC4 is a Protein complex structure of sequences from Paracoccus denitrificans with CU, NA and HEM as ligands. Active as Amine dehydrogenase, with EC number 1.4.99.3 Full crystallographic information is available from OCA.
ReferenceReference
Structure of an electron transfer complex: methylamine dehydrogenase, amicyanin, and cytochrome c551i., Chen L, Durley RC, Mathews FS, Davidson VL, Science. 1994 Apr 1;264(5155):86-90. PMID:8140419
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