7YQA

Crystal structure of D-threonine aldolase from Chlamydomonas reinhardtii

Summary for 7YQA

• Entry DOI: 10.2210/pdb7yqa/pdb
• Descriptor: D-threonine aldolase, MAGNESIUM ION (3 entities in total)
• Functional Keywords: aldolase, plp-dependent enzyme, d-amino acid metabolism, lyase
• Biological source: Chlamydomonas reinhardtii
• Total number of polymer chains: 4
• Total formula weight: 181497.75

Authors

Hirato, Y.,Goto, M.,Mizobuchi, T.,Muramatsu, H.,Tanigawa, M.,Nishimura, K. (deposition date: 2022-08-05, release date: 2023-02-15, Last modification date: 2023-11-29)

Primary citation

Hirato, Y.,Goto, M.,Mizobuchi, T.,Muramatsu, H.,Tanigawa, M.,Nishimura, K.
Structure of pyridoxal 5'-phosphate-bound D-threonine aldolase from Chlamydomonas reinhardtii.
Acta Crystallogr.,Sect.F, 79:31-37, 2023

PubMed Abstract: D-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 β-hydroxy-α-amino acid. This study produced and investigated the crystal structure of DTA from Chlamydomonas reinhardtii (CrDTA) at 1.85 Å 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.

PubMed: 36748339
DOI: 10.1107/S2053230X23000304

Experimental method

X-RAY DIFFRACTION (1.85 Å)