1jbq
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Cystathionine beta-synthase (CBS) is a unique heme- containing enzyme that | + | 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. |
==Disease== | ==Disease== | ||
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[[Category: Janosik, M.]] | [[Category: Janosik, M.]] | ||
[[Category: Kery, V.]] | [[Category: Kery, V.]] | ||
| - | [[Category: Kraus, J | + | [[Category: Kraus, J P.]] |
[[Category: Meier, M.]] | [[Category: Meier, M.]] | ||
[[Category: HEM]] | [[Category: HEM]] | ||
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[[Category: fold type ii of plp enzymes]] | [[Category: fold type ii of plp enzymes]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:20:50 2008'' |
Revision as of 11:20, 21 February 2008
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STRUCTURE OF HUMAN CYSTATHIONINE BETA-SYNTHASE: A UNIQUE PYRIDOXAL 5'-PHOSPHATE DEPENDENT HEMEPROTEIN
Contents |
Overview
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.
Disease
Known diseases associated with this structure: Homocystinuria, B6-responsive and nonresponsive types OMIM:[236200], Thrombosis, hyperhomocysteinemic OMIM:[236200]
About this Structure
1JBQ is a Single protein structure of sequence from Homo sapiens with and as ligands. Active as Cystathionine beta-synthase, with EC number 4.2.1.22 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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