2mta
From Proteopedia
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|PDB= 2mta |SIZE=350|CAPTION= <scene name='initialview01'>2mta</scene>, resolution 2.4Å | |PDB= 2mta |SIZE=350|CAPTION= <scene name='initialview01'>2mta</scene>, resolution 2.4Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> | + | |LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=TRQ:2-AMINO-3-(6,7-DIOXO-6,7-DIHYDRO-1H-INDOL-3-YL)-PROPIONIC+ACID'>TRQ</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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2mta FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mta OCA], [http://www.ebi.ac.uk/pdbsum/2mta PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2mta RCSB]</span> | ||
}} | }} | ||
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[[Category: Chen, L.]] | [[Category: Chen, L.]] | ||
[[Category: Mathews, F S.]] | [[Category: Mathews, F S.]] | ||
| - | [[Category: CU]] | ||
| - | [[Category: HEM]] | ||
| - | [[Category: PO4]] | ||
[[Category: electron transport]] | [[Category: electron transport]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:04:33 2008'' |
Revision as of 01:04, 31 March 2008
| |||||||
| , resolution 2.4Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Activity: | Amine dehydrogenase, with EC number 1.4.99.3 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
Page seeded by OCA on Mon Mar 31 04:04:33 2008
