1s3a

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|ACTIVITY=
|ACTIVITY=
|GENE= NDUFA2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
|GENE= NDUFA2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1s3a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s3a OCA], [http://www.ebi.ac.uk/pdbsum/1s3a PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1s3a RCSB]</span>
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[[Category: nmr]]
[[Category: nmr]]
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Revision as of 20:36, 30 March 2008

Image:1s3a.gif


PDB ID 1s3a

Drag the structure with the mouse to rotate
Gene: NDUFA2 (Homo sapiens)
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



NMR Solution Structure of Subunit B8 from Human NADH-Ubiquinone Oxidoreductase Complex I (CI-B8)


Overview

Subunit B8 from ubiquinone oxidoreductase (complex I) (CI-B8) is one of several nuclear-encoded supernumerary subunits that are not present in bacterial complex I. Its solution structure shows a thioredoxin fold with highest similarities to the human thioredoxin mutant C73S and thioredoxin 2 from Anabeana sp. Interestingly, these proteins contain active sites in the same area, where the disulfide bond of oxidized CI-B8 is located. The redox potential of this disulfide bond is -251.6 mV, comparing well to that of disulfides in other thioredoxin-like proteins. Analysis of the structure reveals a surface area that is exclusively composed of highly conserved residues and thus most likely a subunit interaction site within complex I.

About this Structure

1S3A is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The oxidized subunit B8 from human complex I adopts a thioredoxin fold., Brockmann C, Diehl A, Rehbein K, Strauss H, Schmieder P, Korn B, Kuhne R, Oschkinat H, Structure. 2004 Sep;12(9):1645-54. PMID:15341729

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