Structural insight into gene duplication, gene fusion and domain swapping in the evolution of PLP‐independent amino acid racemases

FEBS Letters

Yohda, Masafumi²  Liu, Lijun¹  Iwata, Kousuke²  Miki, Kunio¹ 

[1] Department of Chemistry, Graduate School of Science, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan;Department of Biotechnology and Life Science, Faculty of Engineering, Tokyo University of Agriculture and Technology, Naka-cho, Koganei, Tokyo 184-8588, Japan

关键词: Aspartate racemase;    Amino acid racemase;    PLP-independent;    Gene duplication and gene fusion;    Domain swapping;    PLP;    pyridoxal 5′-phosphate;    AAR;    amino acid racemase;    AspR;    aspartate racemase;    GluR;    glutamate racemase;    DapE;    diaminopimelate epimerase;    C-domain;    C-terminal domain of P. AspR;    SC-domain;    solely expressed C-terminal domain of P. AspR;   

DOI  :  10.1016/S0014-5793(02)03264-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The X-ray crystal structure has revealed two similar α/β domains of aspartate racemase (AspR) from Pyrococcus horikoshii OT3, and identified a pseudo mirror-symmetric distribution of the residues around its active site [Liu et al. (2002) J. Mol. Biol. 319, 479–489]. Structural homology and functional similarity between the two domains suggested that this enzyme evolved from an ancestral domain by gene duplication and gene fusion. We have expressed solely the C-terminal domain of this AspR and determined its three-dimensional structure by X-ray crystallography. The high structural stability of this domain supports the existence of the ancestral domain. In comparison with other amino acid racemases (AARs), we suggest that gene duplication and gene fusion are conventional ways in the evolution of pyridoxal 5′-phosphate-independent AARs.

【 授权许可】

Unknown