1IU9

Crystal structure of the C-terminal domain of aspartate racemase from Pyrococcus horikoshii OT3

Summary for 1IU9

• Entry DOI: 10.2210/pdb1iu9/pdb
• Related: 1jfl
• Descriptor: aspartate racemase, CALCIUM ION (3 entities in total)
• Functional Keywords: aspartate racemase, c-terminal domain, isomerase
• Biological source: Pyrococcus horikoshii
• Total number of polymer chains: 1
• Total formula weight: 12216.31

Authors

Liu, L.,Iwata, K.,Yohda, M.,Miki, K. (deposition date: 2002-02-28, release date: 2003-09-09, Last modification date: 2024-04-03)

Primary citation

Liu, L.,Iwata, K.,Yohda, M.,Miki, K.
Structural insight into gene duplication, gene fusion and domain swapping in the evolution of PLP-independent amino acid racemases
FEBS LETT., 528:114-118, 2002

PubMed Abstract: The X-ray crystal structure has revealed two similar alpha/beta 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.

PubMed: 12297289
DOI: 10.1016/S0014-5793(02)03264-7

Experimental method

X-RAY DIFFRACTION (2.04 Å)