Literature summary for 2.6.1.52 extracted from

Coulibaly, F.; Lassalle, E.; Baker, H.M.; Baker, E.N.
Structure of phosphoserine aminotransferase from Mycobacterium tuberculosis (2012), Acta Crystallogr. Sect. D, 68, 553-563.

Crystallization (Commentary)

Crystallization (Comment)	Organism
in complex with cofactor pyridoxal 5'-phosphate, to 1.5 A resolution. The enzyme has a fold typical of the aspartate aminotransferase family of pyridoxal phosphate-dependent enzymes. The protein forms a stable symmetrical homodimer which is maintained by extensive interactions, mostly between the large domains of the two subunits. Each active site contains a bound cofactor molecule. The aromatic ring rests above the C-terminal end of the central strand 7 of the seven-stranded beta-sheet in a pocket in which its pyridine N-atom points in towards the interior of the large domain, hydrogen-bonded to the invariant residue Asp176, and its 5'-phosphate and C4 substituent point out into the dimer interface. The phosphate group is adjacent to the N-terminus of helix 3, hydrogen-bonded to the main-chain amide N-atoms of Ala84 and Thr85 and the side chain of Gln199 from one monomer, as well as to Asn251 and Thr252 of the opposing monomer	Mycobacterium tuberculosis

Crystallization (Comment)

Organism

in complex with cofactor pyridoxal 5'-phosphate, to 1.5 A resolution. The enzyme has a fold typical of the aspartate aminotransferase family of pyridoxal phosphate-dependent enzymes. The protein forms a stable symmetrical homodimer which is maintained by extensive interactions, mostly between the large domains of the two subunits. Each active site contains a bound cofactor molecule. The aromatic ring rests above the C-terminal end of the central strand 7 of the seven-stranded beta-sheet in a pocket in which its pyridine N-atom points in towards the interior of the large domain, hydrogen-bonded to the invariant residue Asp176, and its 5'-phosphate and C4 substituent point out into the dimer interface. The phosphate group is adjacent to the N-terminus of helix 3, hydrogen-bonded to the main-chain amide N-atoms of Ala84 and Thr85 and the side chain of Gln199 from one monomer, as well as to Asn251 and Thr252 of the opposing monomer

Mycobacterium tuberculosis

Organism

Organism	UniProt	Comment	Textmining
Mycobacterium tuberculosis	P9WQ73	-	-
Mycobacterium tuberculosis H37Rv	P9WQ73	-	-

Synonyms

Synonyms	Comment	Organism
PSAT	-	Mycobacterium tuberculosis
serC	-	Mycobacterium tuberculosis

Cofactor

Cofactor	Comment	Organism	Structure
pyridoxal 5'-phosphate	-	Mycobacterium tuberculosis

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Release 2023.1 (January 2023)