Abstract：
: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.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Chen L,Durley R,Poliks BJ,Hamada K,Chen Z,Mathews FS,Davidson VL,Satow Y,Huizinga E,Vellieux FMdoi
10.1021/bi00136a006subject
Has Abstract,Author List Incompletepub_date
1992-06-02 00:00:00pages
4959-64issue
21eissn
0006-2960issn
1520-4995journal_volume
31pub_type
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