期刊
PROTEIN SCIENCE
卷 12, 期 5, 页码 1109-1118出版社
COLD SPRING HARBOR LAB PRESS, PUBLICATIONS DEPT
DOI: 10.1110/ps.0238103
关键词
FAD dependent sulfhydryl oxidase; augmenter of liver regeneration; crystal structure; ERV2
资金
- NIDDK NIH HHS [R01 DK032303] Funding Source: Medline
The crystal structure of recombinant rat augmenter of liver regeneration (ALRp) has been determined to 1.8 Angstrom. 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.
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