3PC4

Full length structure of cystathionine beta-synthase from Drosophila in complex with serine

3PC4 の概要

• エントリーDOI: 10.2210/pdb3pc4/pdb
• 関連するPDBエントリー: 3PC2 3PC3
• 分子名称: CG1753, isoform A, PROTOPORPHYRIN IX CONTAINING FE, (E)-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-serine, ... (5 entities in total)
• 機能のキーワード: cbs, synthase, plp, heme, carbanion, lyase
• 由来する生物種: Drosophila melanogaster (Fruit fly)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 58443.51

構造登録者

Koutmos, M.,Smith, J.L. (登録日: 2010-10-21, 公開日: 2010-12-01, 最終更新日: 2023-09-06)

主引用文献

Koutmos, M.,Kabil, O.,Smith, J.L.,Banerjee, R.
Structural basis for substrate activation and regulation by cystathionine beta-synthase (CBS) domains in cystathionine {beta}-synthase.
Proc.Natl.Acad.Sci.USA, 107:20958-20963, 2010

PubMed Abstract: The catalytic potential for H(2)S biogenesis and homocysteine clearance converge at the active site of cystathionine β-synthase (CBS), a pyridoxal phosphate-dependent enzyme. CBS catalyzes β-replacement reactions of either serine or cysteine by homocysteine to give cystathionine and water or H(2)S, respectively. In this study, high-resolution structures of the full-length enzyme from Drosophila in which a carbanion (1.70 Å) and an aminoacrylate intermediate (1.55 Å) have been captured are reported. Electrostatic stabilization of the zwitterionic carbanion intermediate is afforded by the close positioning of an active site lysine residue that is initially used for Schiff base formation in the internal aldimine and later as a general base. Additional stabilizing interactions between active site residues and the catalytic intermediates are observed. Furthermore, the structure of the regulatory "energy-sensing" CBS domains, named after this protein, suggests a mechanism for allosteric activation by S-adenosylmethionine.

PubMed: 21081698
DOI: 10.1073/pnas.1011448107

実験手法

X-RAY DIFFRACTION (1.7 Å)