1jbq
From Proteopedia
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|PDB= 1jbq |SIZE=350|CAPTION= <scene name='initialview01'>1jbq</scene>, resolution 2.60Å | |PDB= 1jbq |SIZE=350|CAPTION= <scene name='initialview01'>1jbq</scene>, resolution 2.60Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> and <scene name='pdbligand=PLP:PYRIDOXAL-5 | + | |LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> and <scene name='pdbligand=PLP:PYRIDOXAL-5'-PHOSPHATE'>PLP</scene> |
|ACTIVITY= [http://en.wikipedia.org/wiki/Cystathionine_beta-synthase Cystathionine beta-synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.22 4.2.1.22] | |ACTIVITY= [http://en.wikipedia.org/wiki/Cystathionine_beta-synthase Cystathionine beta-synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.22 4.2.1.22] | ||
|GENE= | |GENE= | ||
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[[Category: fold type ii of plp enzyme]] | [[Category: fold type ii of plp enzyme]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 12:19:29 2008'' |
Revision as of 10:19, 23 March 2008
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| , resolution 2.60Å | |||||||
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| Ligands: | and | ||||||
| Activity: | Cystathionine beta-synthase, with EC number 4.2.1.22 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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