1mda
From Proteopedia
(New page: 200px<br /><applet load="1mda" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mda, resolution 2.5Å" /> '''CRYSTAL STRUCTURE OF ...) |
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| - | [[Image:1mda.gif|left|200px]]<br /><applet load="1mda" size=" | + | [[Image:1mda.gif|left|200px]]<br /><applet load="1mda" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1mda, resolution 2.5Å" /> | caption="1mda, resolution 2.5Å" /> | ||
'''CRYSTAL STRUCTURE OF AN ELECTRON-TRANSFER COMPLEX BETWEEN METHYLAMINE DEHYDROGENASE AND AMICYANIN'''<br /> | '''CRYSTAL STRUCTURE OF AN ELECTRON-TRANSFER COMPLEX BETWEEN METHYLAMINE DEHYDROGENASE AND AMICYANIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of the complex between the quinoprotein methylamine | + | 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== | ==About this Structure== | ||
| - | 1MDA is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Paracoccus_denitrificans Paracoccus denitrificans] with CU as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http:// | + | 1MDA is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Paracoccus_denitrificans Paracoccus denitrificans] with <scene name='pdbligand=CU:'>CU</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MDA OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Chen, L.]] | [[Category: Chen, L.]] | ||
[[Category: Durley, R.]] | [[Category: Durley, R.]] | ||
| - | [[Category: Mathews, F | + | [[Category: Mathews, F S.]] |
[[Category: CU]] | [[Category: CU]] | ||
[[Category: electron transport]] | [[Category: electron transport]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:54:05 2008'' |
Revision as of 11:54, 21 February 2008
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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 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
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