1iu9 | pdb_00001iu9

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

spinqualitylabelsall models 1iu9, resolution 2.04Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1iu9 is a 1 chain structure with sequence from Pyrho. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA Related: 1jfl Gene: pPH0670E (PYRHO) Activity: Aspartate racemase, with EC number 5.1.1.13 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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