1TDJ

THREONINE DEAMINASE (BIOSYNTHETIC) FROM E. COLI

Summary for 1TDJ

• Entry DOI: 10.2210/pdb1tdj/pdb
• Descriptor: BIOSYNTHETIC THREONINE DEAMINASE, PYRIDOXAL-5'-PHOSPHATE (3 entities in total)
• Functional Keywords: allostery, cooperative, tetramer, regulation, pyridoxal phosphate, isoleucine biosynthesis
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 56510.21

Authors

Gallagher, D.T.,Gilliland, G.L.,Xiao, G.,Eisenstein, E. (deposition date: 1998-03-27, release date: 1998-10-14, Last modification date: 2025-03-26)

Primary citation

Gallagher, D.T.,Gilliland, G.L.,Xiao, G.,Zondlo, J.,Fisher, K.E.,Chinchilla, D.,Eisenstein, E.
Structure and control of pyridoxal phosphate dependent allosteric threonine deaminase.
Structure, 6:465-475, 1998

PubMed Abstract: Feedback inhibition of biosynthetic threonine deaminase (TD) from Escherichia coli provided one of the earliest examples of protein-based metabolic regulation. Isoleucine, the pathway end-product, and valine, the product of a parallel pathway, serve as allosteric inhibitor and activator, respectively. This enzyme is thus a useful model system for studying the structural basis of allosteric control mechanisms.

PubMed: 9562556
DOI: 10.1016/S0969-2126(98)00048-3

Experimental method

X-RAY DIFFRACTION (2.8 Å)