1oqc

The crystal structure of augmenter of liver regeneration: a mammalian FAD dependent sulfhydryl oxidaseThe crystal structure of augmenter of liver regeneration: a mammalian FAD dependent sulfhydryl oxidase

Structural highlights

1oqc is a 4 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.8Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ALR_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 PubMed

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 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

↑ Hagiya M, Francavilla A, Polimeno L, Ihara I, Sakai H, Seki T, Shimonishi M, Porter KA, Starzl TE. Cloning and sequence analysis of the rat augmenter of liver regeneration (ALR) gene: expression of biologically active recombinant ALR and demonstration of tissue distribution. Proc Natl Acad Sci U S A. 1994 Aug 16;91(17):8142-6. PMID:8058770
↑ Wu CK, Dailey TA, Dailey HA, Wang BC, Rose JP. The crystal structure of augmenter of liver regeneration: A mammalian FAD-dependent sulfhydryl oxidase. Protein Sci. 2003 May;12(5):1109-18. PMID:12717032

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OCA

[1] Hagiya M, Francavilla A, Polimeno L, Ihara I, Sakai H, Seki T, Shimonishi M, Porter KA, Starzl TE. Cloning and sequence analysis of the rat augmenter of liver regeneration (ALR) gene: expression of biologically active recombinant ALR and demonstration of tissue distribution. Proc Natl Acad Sci U S A. 1994 Aug 16;91(17):8142-6. PMID:8058770

[2] Wu CK, Dailey TA, Dailey HA, Wang BC, Rose JP. The crystal structure of augmenter of liver regeneration: A mammalian FAD-dependent sulfhydryl oxidase. Protein Sci. 2003 May;12(5):1109-18. PMID:12717032

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