1oqc
The crystal structure of augmenter of liver regeneration: a mammalian FAD dependent sulfhydryl oxidase
Structural highlights
FunctionALR_RAT FAD-dependent sulfhydryl oxidase that catalyzes disulfide bond formation. Within the mitochondrial intermembrane space, participates in a chain of disulfide exchange reactions with MIA40, that generate disulfide bonds in a number of resident proteins with twin Cx3C and Cx9C motifs. May have a function in liver regeneration and spermatogenesis.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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 reveals a number of significant structural differences, which are related to the in vivo functions of these two proteins. Possible physiological roles of ALR are examined and a hypothesis that it may serve multiple roles is proposed. 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:012717032[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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