2mta
From Proteopedia
(New page: 200px<br /><applet load="2mta" size="450" color="white" frame="true" align="right" spinBox="true" caption="2mta, resolution 2.4Å" /> '''CRYSTAL STRUCTURE OF ...) |
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| - | [[Image:2mta.jpg|left|200px]]<br /><applet load="2mta" size=" | + | [[Image:2mta.jpg|left|200px]]<br /><applet load="2mta" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2mta, resolution 2.4Å" /> | caption="2mta, resolution 2.4Å" /> | ||
'''CRYSTAL STRUCTURE OF A TERNARY ELECTRON TRANSFER COMPLEX BETWEEN METHYLAMINE DEHYDROGENASE, AMICYANIN AND A C-TYPE CYTOCHROME'''<br /> | '''CRYSTAL STRUCTURE OF A TERNARY ELECTRON TRANSFER COMPLEX BETWEEN METHYLAMINE DEHYDROGENASE, AMICYANIN AND A C-TYPE CYTOCHROME'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of a ternary protein complex has been determined at | + | The crystal structure of a ternary protein complex has been determined at 2.4 angstrom resolution. The complex is composed of three electron transfer proteins from Paracoccus denitrificans, the quinoprotein methylamine dehydrogenase, the blue copper protein amicyanin, and the cytochrome c551i. The central region of the c551i is folded similarly to several small bacterial c-type cytochromes; there is a 45-residue extension at the amino terminus and a 25-residue extension at the carboxyl terminus. The methylamine dehydrogenase-amicyanin interface is largely hydrophobic, whereas the amicyanin-cytochrome interface is more polar, with several charged groups present on each surface. Analysis of the simplest electron transfer pathways between the redox partners points out the importance of other factors such as energetics in determining the electron transfer rates. |
==About this Structure== | ==About this Structure== | ||
| - | 2MTA 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, PO4 and HEM as [http://en.wikipedia.org/wiki/ligands ligands]. 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:// | + | 2MTA 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>, <scene name='pdbligand=PO4:'>PO4</scene> and <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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=2MTA OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Chen, L.]] | [[Category: Chen, L.]] | ||
| - | [[Category: Mathews, F | + | [[Category: Mathews, F S.]] |
[[Category: CU]] | [[Category: CU]] | ||
[[Category: HEM]] | [[Category: HEM]] | ||
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[[Category: electron transport]] | [[Category: electron transport]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:07:56 2008'' |
Revision as of 16:08, 21 February 2008
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CRYSTAL STRUCTURE OF A TERNARY ELECTRON TRANSFER COMPLEX BETWEEN METHYLAMINE DEHYDROGENASE, AMICYANIN AND A C-TYPE CYTOCHROME
Overview
The crystal structure of a ternary protein complex has been determined at 2.4 angstrom resolution. The complex is composed of three electron transfer proteins from Paracoccus denitrificans, the quinoprotein methylamine dehydrogenase, the blue copper protein amicyanin, and the cytochrome c551i. The central region of the c551i is folded similarly to several small bacterial c-type cytochromes; there is a 45-residue extension at the amino terminus and a 25-residue extension at the carboxyl terminus. The methylamine dehydrogenase-amicyanin interface is largely hydrophobic, whereas the amicyanin-cytochrome interface is more polar, with several charged groups present on each surface. Analysis of the simplest electron transfer pathways between the redox partners points out the importance of other factors such as energetics in determining the electron transfer rates.
About this Structure
2MTA is a Protein complex structure of sequences from Paracoccus denitrificans with , and as ligands. Active as Amine dehydrogenase, with EC number 1.4.99.3 Full crystallographic information is available from OCA.
Reference
Structure of an electron transfer complex: methylamine dehydrogenase, amicyanin, and cytochrome c551i., Chen L, Durley RC, Mathews FS, Davidson VL, Science. 1994 Apr 1;264(5155):86-90. PMID:8140419
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