5b19

Picrophilus torridus aspartate racemase

spinqualitylabelsall models 5b19, resolution 1.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5b19 is a 2 chain structure with sequence from Picrophilus torridus DSM 9790. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.851Å Ligands: TLA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q6L2R8_PICTO Publication Abstract from PubMed Functional and structural characterizations of pyridoxal 5'-phosphate-independent aspartate racemase of the acidothermophilic archaeon Picrophilus torridus were performed. Picrophilus aspartate racemase exhibited high substrate specificity to aspartic acid. The optimal reaction temperature was 60 degrees C, which is almost the same as the optimal growth temperature. Reflecting the low pH in the cytosol, the optimal reaction pH of Picrophilus aspartate racemase was approximately 5.5. However, the activity at the putative cytosolic pH of 4.6 was approximately 6 times lower than that at the optimal pH of 5.5. The crystal structure of Picrophilus aspartate racemase was almost the same as that of other pyridoxal 5'-phosphate -independent aspartate racemases. In two molecules of the dimer, one molecule contained a tartaric acid molecule in the catalytic site; the structure of the other molecule was relatively flexible. Finally, we examined the intracellular existence of D-amino acids. Unexpectedly, the proportion of D-aspartate to total aspartate was not very high. In contrast, both D-proline and D-alanine were observed. Because Picrophilus aspartate racemase is highly specific to aspartate, other amino acid racemases might exist in Picrophilus torridus. Structural and functional characterization of aspartate racemase from the acidothermophilic archaeon Picrophilus torridus.,Aihara T, Ito T, Yamanaka Y, Noguchi K, Odaka M, Sekine M, Homma H, Yohda M Extremophiles. 2016 Apr 19. PMID:27094682 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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