1jbq

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{{STRUCTURE_1jbq| PDB=1jbq | SCENE= }}
{{STRUCTURE_1jbq| PDB=1jbq | SCENE= }}
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'''STRUCTURE OF HUMAN CYSTATHIONINE BETA-SYNTHASE: A UNIQUE PYRIDOXAL 5'-PHOSPHATE DEPENDENT HEMEPROTEIN'''
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===STRUCTURE OF HUMAN CYSTATHIONINE BETA-SYNTHASE: A UNIQUE PYRIDOXAL 5'-PHOSPHATE DEPENDENT HEMEPROTEIN===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 11483494 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11483494}}
==About this Structure==
==About this Structure==
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[[Category: Meier, M.]]
[[Category: Meier, M.]]
[[Category: Fold type ii of plp enzyme]]
[[Category: Fold type ii of plp enzyme]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:01:37 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 19:59:12 2008''

Revision as of 16:59, 1 July 2008

Image:1jbq.png

Template:STRUCTURE 1jbq

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

Template:ABSTRACT PUBMED 11483494

About this Structure

1JBQ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structure of human cystathionine beta-synthase: a unique pyridoxal 5'-phosphate-dependent heme protein., Meier M, Janosik M, Kery V, Kraus JP, Burkhard P, EMBO J. 2001 Aug 1;20(15):3910-6. PMID:11483494

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