1mda

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{{STRUCTURE_1mda| PDB=1mda | SCENE= }}
{{STRUCTURE_1mda| PDB=1mda | SCENE= }}
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'''CRYSTAL STRUCTURE OF AN ELECTRON-TRANSFER COMPLEX BETWEEN METHYLAMINE DEHYDROGENASE AND AMICYANIN'''
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===CRYSTAL STRUCTURE OF AN ELECTRON-TRANSFER COMPLEX BETWEEN METHYLAMINE DEHYDROGENASE AND AMICYANIN===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_1599920}}
==About this Structure==
==About this Structure==
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[[Category: Mathews, F S.]]
[[Category: Mathews, F S.]]
[[Category: Electron transport]]
[[Category: Electron transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 23:43:28 2008''

Revision as of 20:43, 2 July 2008

Image:1mda.png

Template:STRUCTURE 1mda

CRYSTAL STRUCTURE OF AN ELECTRON-TRANSFER COMPLEX BETWEEN METHYLAMINE DEHYDROGENASE AND AMICYANIN

Template:ABSTRACT PUBMED 1599920

About this Structure

1MDA is a Protein complex structure of sequences from Paracoccus denitrificans. 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

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