5AVO

Crystal structure of the reduced form of homoserine dehydrogenase from Sulfolobus tokodaii.

Summary for 5AVO

Entry DOI	10.2210/pdb5avo/pdb
Related	4YDR
Descriptor	Homoserine dehydrogenase (2 entities in total)
Functional Keywords	reduced form, oxidoreductase
Biological source	Sulfolobus tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
Total number of polymer chains	2
Total formula weight	66822.99
Authors	Goto, M.,Yoshimune, K.,Kaneko, R. (deposition date: 2015-06-25, release date: 2015-11-11, Last modification date: 2024-11-06)
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 Cited by 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 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.8 Å)

Structure validation