1CJ0

CRYSTAL STRUCTURE OF RABBIT CYTOSOLIC SERINE HYDROXYMETHYLTRANSFERASE AT 2.8 ANGSTROM RESOLUTION

1CJ0 の概要

• エントリーDOI: 10.2210/pdb1cj0/pdb
• 分子名称: PROTEIN (SERINE HYDROXYMETHYLTRANSFERASE), PYRIDOXAL-5'-PHOSPHATE (3 entities in total)
• 機能のキーワード: hydroxymethyl transferase, 1 carbon metabolism, transferase
• 由来する生物種: Oryctolagus cuniculus (rabbit)
• 細胞内の位置: Cytoplasm: P07511
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 103907.85

構造登録者

Scarsdale, J.N.,Kazanina, G.,Radaev, S.,Schirch, V.,Wright, H.T. (登録日: 1999-04-20, 公開日: 1999-05-06, 最終更新日: 2023-12-27)

主引用文献

Scarsdale, J.N.,Kazanina, G.,Radaev, S.,Schirch, V.,Wright, H.T.
Crystal structure of rabbit cytosolic serine hydroxymethyltransferase at 2.8 A resolution: mechanistic implications.
Biochemistry, 38:8347-8358, 1999

PubMed Abstract: Serine hydroxymethyltransferase (SHMT) catalyzes the reversible cleavage of serine to form glycine and single carbon groups that are essential for many biosynthetic pathways. SHMT requires both pyridoxal phosphate (PLP) and tetrahydropteroylpolyglutamate (H4PteGlun) as cofactors, the latter as a carrier of the single carbon group. We describe here the crystal structure at 2.8 A resolution of rabbit cytosolic SHMT (rcSHMT) in two forms: one with the PLP covalently bound as an aldimine to the Nepsilon-amino group of the active site lysine and the other with the aldimine reduced to a secondary amine. The rcSHMT structure closely resembles the structure of human SHMT, confirming its similarity to the alpha-class of PLP enzymes. The structures reported here further permit identification of changes in the PLP group that accompany formation of the geminal diamine complex, the first intermediate in the reaction pathway. On the basis of the current mechanism derived from solution studies and the properties of site mutants, we are able to model the binding of both the serine substrate and the H4PteGlun cofactor. This model explains the properties of several site mutants of SHMT and offers testable hypotheses for a more detailed mechanism of this enzyme.

PubMed: 10387080
DOI: 10.1021/bi9904151

実験手法

X-RAY DIFFRACTION (2.8 Å)