1mda
From Proteopedia
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| - | [[Image:1mda.gif|left|200px]] | + | [[Image:1mda.gif|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF AN ELECTRON-TRANSFER COMPLEX BETWEEN METHYLAMINE DEHYDROGENASE AND AMICYANIN''' | + | {{Structure |
| + | |PDB= 1mda |SIZE=350|CAPTION= <scene name='initialview01'>1mda</scene>, resolution 2.5Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CU:COPPER (II) ION'>CU</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Amine_dehydrogenase Amine dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.99.3 1.4.99.3] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF AN ELECTRON-TRANSFER COMPLEX BETWEEN METHYLAMINE DEHYDROGENASE AND AMICYANIN''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1MDA is a [ | + | 1MDA is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Paracoccus_denitrificans Paracoccus denitrificans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MDA OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/1599920 1599920] |
[[Category: Amine dehydrogenase]] | [[Category: Amine dehydrogenase]] | ||
[[Category: Paracoccus denitrificans]] | [[Category: Paracoccus denitrificans]] | ||
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[[Category: electron transport]] | [[Category: electron transport]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:42:03 2008'' |
Revision as of 10:42, 20 March 2008
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| , resolution 2.5Å | |||||||
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| Ligands: | |||||||
| Activity: | Amine dehydrogenase, with EC number 1.4.99.3 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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 Thu Mar 20 12:42:03 2008
