1mda
From Proteopedia
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CRYSTAL STRUCTURE OF AN ELECTRON-TRANSFER COMPLEX BETWEEN METHYLAMINE DEHYDROGENASE AND AMICYANIN
Overview
The crystal structure of the complex between the quinoprotein methylamine, dehydrogenase (MADH) and the type I blue copper protein amicyanin, both, from Paracoccus denitrificans, has been determined at 2.5-A resolution, using molecular replacement. The search model was MADH from Thiobacillus, versutus. The amicyanin could be located in an averaged electron density, difference map and the model improved by refinement and model building, procedures. Nine beta-strands are observed within the amicyanin molecule., The copper atom is located between three antiparallel strands and is about, 2.5 A below the protein surface. The major intermolecular interactions, occur between amicyanin and the light subunit of MADH where the interface, is largely hydrophobic. The copper atom of amicyanin and the redox, cofactor of MADH are about 9.4 A apart. One of the copper ligands, His 95, lies between the two redox centers and may facilitate electron transfer, between them.
About this Structure
1MDA is a Protein complex structure of sequences from Paracoccus denitrificans with CU as ligand. Active as Amine dehydrogenase, with EC number 1.4.99.3 Full crystallographic information is available from OCA.
Reference
Crystal structure of an electron-transfer complex between methylamine dehydrogenase and amicyanin., Chen L, Durley R, Poliks BJ, Hamada K, Chen Z, Mathews FS, Davidson VL, Satow Y, Huizinga E, Vellieux FM, et al., Biochemistry. 1992 Jun 2;31(21):4959-64. PMID:1599920
Page seeded by OCA on Tue Nov 20 21:20:31 2007
