1oqc
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The crystal structure of augmenter of liver regeneration: a mammalian FAD dependent sulfhydryl oxidase
OverviewOverview
The crystal structure of recombinant rat augmenter of liver regeneration, (ALRp) has been determined to 1.8 A. The protein is a homodimer, stabilized by extensive noncovalent interactions and a network of hydrogen, bonds, and possesses a noncovalently bound FAD in a motif previously found, only in the related protein ERV2p. ALRp functions in vitro as a disulfide, oxidase using dithiothreitol as reductant. Reduction of the flavin by DTT, occurs under aerobic conditions resulting in a spectrum characteristic of, a neutral semiquinone. This semiquinone is stable and is only fully, reduced by addition of dithionite. Mutation of either of two cysteine, residues that are located adjacent to the FAD results in inactivation of, the oxidase activity. A comparison of ALRp with ERV2p is made that ... [(full description)]
About this StructureAbout this Structure
1OQC is a [Single protein] structure of sequence from [Rattus norvegicus] with FAD as [ligand]. Full crystallographic information is available from [OCA].
ReferenceReference
The crystal structure of augmenter of liver regeneration: A mammalian FAD-dependent sulfhydryl oxidase., Wu CK, Dailey TA, Dailey HA, Wang BC, Rose JP, Protein Sci. 2003 May;12(5):1109-18. PMID:12717032
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