1JBQ

STRUCTURE OF HUMAN CYSTATHIONINE BETA-SYNTHASE: A UNIQUE PYRIDOXAL 5'-PHOSPHATE DEPENDENT HEMEPROTEIN

1JBQ の概要

• エントリーDOI: 10.2210/pdb1jbq/pdb
• 関連するPDBエントリー: 1D6S
• 分子名称: CYSTATHIONINE BETA-SYNTHASE, PROTOPORPHYRIN IX CONTAINING FE, PYRIDOXAL-5'-PHOSPHATE, ... (4 entities in total)
• 機能のキーワード: fold type ii of plp enzymes, lyase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: P35520
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 290302.22

構造登録者

Meier, M.,Janosik, M.,Kery, V.,Kraus, J.P.,Burkhard, P. (登録日: 2001-06-06, 公開日: 2001-08-12, 最終更新日: 2023-08-16)

主引用文献

Meier, M.,Janosik, M.,Kery, V.,Kraus, J.P.,Burkhard, P.
Structure of human cystathionine beta-synthase: a unique pyridoxal 5'-phosphate-dependent heme protein.
EMBO J., 20:3910-3916, 2001

PubMed Abstract: Cystathionine beta-synthase (CBS) is a unique heme- containing enzyme that catalyzes a pyridoxal 5'-phosphate (PLP)-dependent condensation of serine and homocysteine to give cystathionine. Deficiency of CBS leads to homocystinuria, an inherited disease of sulfur metabolism characterized by increased levels of the toxic metabolite homocysteine. Here we present the X-ray crystal structure of a truncated form of the enzyme. CBS shares the same fold with O-acetylserine sulfhydrylase but it contains an additional N-terminal heme binding site. This heme binding motif together with a spatially adjacent oxidoreductase active site motif could explain the regulation of its enzyme activity by redox changes.

PubMed: 11483494
DOI: 10.1093/emboj/20.15.3910

実験手法

X-RAY DIFFRACTION (2.6 Å)