1JBQ

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

Summary for 1JBQ

• Entry DOI: 10.2210/pdb1jbq/pdb
• Related: 1D6S
• Descriptor: CYSTATHIONINE BETA-SYNTHASE, PROTOPORPHYRIN IX CONTAINING FE, PYRIDOXAL-5'-PHOSPHATE, ... (4 entities in total)
• Functional Keywords: fold type ii of plp enzymes, lyase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: P35520
• Total number of polymer chains: 6
• Total formula weight: 290302.22

Authors

Meier, M.,Janosik, M.,Kery, V.,Kraus, J.P.,Burkhard, P. (deposition date: 2001-06-06, release date: 2001-08-12, Last modification date: 2023-08-16)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.6 Å)