4YDR

Crystal structure of oxidized homoserine dehydrogenase of Sulfolobus tokodaii

Summary for 4YDR

• Entry DOI: 10.2210/pdb4ydr/pdb
• Descriptor: Homoserine dehydrogenase, SODIUM ION (3 entities in total)
• Functional Keywords: oxidized form, oxidoreductase
• Biological source: Sulfolobus tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
• Total number of polymer chains: 2
• Total formula weight: 66845.98

Authors

Goto, M.,Yoshimune, K.,Kaneko, R. (deposition date: 2015-02-23, release date: 2015-11-11, Last modification date: 2024-10-30)

Primary citation

Tomonaga, Y.,Kaneko, R.,Goto, M.,Ohshima, T.,Yoshimune, K.
Structural insight into activation of homoserine dehydrogenase from the archaeonSulfolobus tokodaiivia reduction.
Biochem Biophys Rep, 3:14-17, 2015

PubMed Abstract: Homoserine dehydrogenase (HSD; 305 amino acid residues) catalyzes an NAD(P)-dependent reversible reaction between l-homoserine and aspartate 4-semialdehyde and is involved in the aspartate pathway. HSD from the hyperthermophilic archaeon was markedly activated (2.5-fold) by the addition of 0.8 mM dithiothreitol. The crystal structure of the homodimer indicated that the activation was caused by cleavage of the disulfide bond formed between two cysteine residues (C303) in the C-terminal regions of the two subunits.

PubMed: 29124164
DOI: 10.1016/j.bbrep.2015.07.006

Experimental method

X-RAY DIFFRACTION (1.6 Å)