6d6z

Structure of the malate racemase apoprotein from Thermoanaerobacterium thermosaccharolyticum

spinqualitylabelsall models 6d6z, resolution 2.38Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6d6z is a 1 chain structure with sequence from Thermoanaerobacterium thermosaccharolyticum DSM 571. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.38Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function D9TSN9_THETC Publication Abstract from PubMed Isomerization reactions are fundamental in biology. Lactate racemase, which isomerizes L- and D-lactate, is composed of the LarA protein and a nickel-containing cofactor, the nickel-pincer nucleotide (NPN). In this study, we show that LarA is part of a superfamily containing many different enzymes. We overexpressed and purified 13 lactate racemase homologs, incorporated the NPN cofactor, and assayed the isomerization of different substrates guided by gene context analysis. We discovered two malate racemases, one phenyllactate racemase, one alpha-hydroxyglutarate racemase, two D-gluconate 2-epimerases, and one short-chain aliphatic alpha-hydroxyacid racemase among the tested enzymes. We solved the structure of a malate racemase apoprotein and used it, along with the previously described structures of lactate racemase holoprotein and D-gluconate epimerase apoprotein, to identify key residues involved in substrate binding. This study demonstrates that the NPN cofactor is used by a diverse superfamily of alpha-hydroxyacid racemases and epimerases, widely expanding the scope of NPN-dependent enzymes. Uncovering a superfamily of nickel-dependent hydroxyacid racemases and epimerases.,Desguin B, Urdiain-Arraiza J, Da Costa M, Fellner M, Hu J, Hausinger RP, Desmet T, Hols P, Soumillion P Sci Rep. 2020 Oct 22;10(1):18123. doi: 10.1038/s41598-020-74802-6. PMID:33093595 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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