2fug: Difference between revisions

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Crystal structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus

OverviewOverview

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 StructureAbout this Structure

2FUG is a Protein complex structure of sequences from Thermus thermophilus with , and as ligands. Active as NADH dehydrogenase (quinone), with EC number 1.6.99.5 Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Thu Feb 21 17:25:13 2008

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-[[Image:2fug.gif|left|200px]]<br /><applet load="2fug" size="450" color="white" frame="true" align="right" spinBox="true"
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 caption="2fug, resolution 3.300&Aring;" />
 '''Crystal structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus'''<br />
 ==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.
+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==
-FUG is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with SF4, FES and FMN as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2FUG OCA].
+FUG is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with <scene name='pdbligand=SF4:'>SF4</scene>, <scene name='pdbligand=FES:'>FES</scene> and <scene name='pdbligand=FMN:'>FMN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FUG OCA].
 ==Reference==
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 [[Category: Thermus thermophilus]]
 [[Category: Hinchliffe, P.]]
-[[Category: Sazanov, L.A.]]
+[[Category: Sazanov, L A.]]
 [[Category: FES]]
 [[Category: FMN]]
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 [[Category: respiratory chain]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 10:46:45 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:25:13 2008''