2fug
From Proteopedia
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|PDB= 2fug |SIZE=350|CAPTION= <scene name='initialview01'>2fug</scene>, resolution 3.300Å | |PDB= 2fug |SIZE=350|CAPTION= <scene name='initialview01'>2fug</scene>, resolution 3.300Å | ||
|SITE= | |SITE= | ||
- | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene> |
- | |ACTIVITY= [http://en.wikipedia.org/wiki/NADH_dehydrogenase_(quinone) NADH dehydrogenase (quinone)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.99.5 1.6.99.5] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/NADH_dehydrogenase_(quinone) NADH dehydrogenase (quinone)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.99.5 1.6.99.5] </span> |
|GENE= | |GENE= | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY= | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fug FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fug OCA], [http://www.ebi.ac.uk/pdbsum/2fug PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2fug RCSB]</span> | ||
}} | }} | ||
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[[Category: Hinchliffe, P.]] | [[Category: Hinchliffe, P.]] | ||
[[Category: Sazanov, L A.]] | [[Category: Sazanov, L A.]] | ||
- | [[Category: FES]] | ||
- | [[Category: FMN]] | ||
- | [[Category: SF4]] | ||
[[Category: electron transport]] | [[Category: electron transport]] | ||
[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
[[Category: respiratory chain]] | [[Category: respiratory chain]] | ||
- | ''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 03:07:52 2008'' |
Revision as of 00:07, 31 March 2008
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, resolution 3.300Å | |||||||
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Ligands: | , , | ||||||
Activity: | NADH dehydrogenase (quinone), with EC number 1.6.99.5 | ||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Crystal structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus
Overview
Respiratory complex I plays a central role in cellular energy production in bacteria and mitochondria. Its dysfunction is implicated in many human neurodegenerative diseases, as well as in aging. The crystal structure of the hydrophilic domain (peripheral arm) of complex I from Thermus thermophilus has been solved at 3.3 angstrom resolution. This subcomplex consists of eight subunits and contains all the redox centers of the enzyme, including nine iron-sulfur clusters. The primary electron acceptor, flavin-mononucleotide, is within electron transfer distance of cluster N3, leading to the main redox pathway, and of the distal cluster N1a, a possible antioxidant. The structure reveals new aspects of the mechanism and evolution of the enzyme. The terminal cluster N2 is coordinated, uniquely, by two consecutive cysteines. The novel subunit Nqo15 has a similar fold to the mitochondrial iron chaperone frataxin, and it may be involved in iron-sulfur cluster regeneration in the complex.
About this Structure
2FUG is a Protein complex structure of sequences from Thermus thermophilus. Full crystallographic information is available from OCA.
Reference
Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus., Sazanov LA, Hinchliffe P, Science. 2006 Mar 10;311(5766):1430-6. Epub 2006 Feb 9. PMID:16469879
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