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Structural insight into gene duplication, gene fusion and domain swapping in the evolution of PLP‐independent amino acid racemases
Author(s) -
Liu Lijun,
Iwata Kousuke,
Yohda Masafumi,
Miki Kunio
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)03264-7
Subject(s) - gene duplication , gene , amino acid , fusion gene , genetics , domain (mathematical analysis) , chemistry , biology , computational biology , biochemistry , mathematical analysis , mathematics
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.