1iu9
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Crystal structure of the C-terminal domain of aspartate racemase from Pyrococcus horikoshii OT3
OverviewOverview
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.
About this StructureAbout this Structure
1IU9 is a Single protein structure of sequence from Pyrococcus horikoshii with CA as ligand. Active as Aspartate racemase, with EC number 5.1.1.13 Full crystallographic information is available from OCA.
ReferenceReference
Structural insight into gene duplication, gene fusion and domain swapping in the evolution of PLP-independent amino acid racemases., Liu L, Iwata K, Yohda M, Miki K, FEBS Lett. 2002 Sep 25;528(1-3):114-8. PMID:12297289
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