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Crystal structure of D-threonine aldolase from Chlamydomonas reinhardtiiCrystal structure of D-threonine aldolase from Chlamydomonas reinhardtii
Structural highlights
FunctionPublication Abstract from PubMedD-Threonine aldolase (DTA) is a pyridoxal-5'-phosphate-dependent enzyme which catalyzes the reversible aldol reaction of glycine with a corresponding aldehyde to yield the D-form beta-hydroxy-alpha-amino acid. This study produced and investigated the crystal structure of DTA from Chlamydomonas reinhardtii (CrDTA) at 1.85 A resolution. To our knowledge, this is the first report on the crystal structure of eukaryotic DTA. Compared with the structure of bacterial DTA, CrDTA has a similar arrangement of active-site residues. On the other hand, we speculated that some non-conserved residues alter the affinity for substrates and inhibitors. The structure of CrDTA could provide insights into the structural framework for structure-guided protein engineering studies to modify reaction selectivity. Structure of pyridoxal 5'-phosphate-bound D-threonine aldolase from Chlamydomonas reinhardtii.,Hirato Y, Goto M, Mizobuchi T, Muramatsu H, Tanigawa M, Nishimura K Acta Crystallogr F Struct Biol Commun. 2023 Feb 1;79(Pt 2):31-37. doi: , 10.1107/S2053230X23000304. Epub 2023 Feb 2. PMID:36748339[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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