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> | + | |LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <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= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1d6s|1D6S]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jbq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jbq OCA], [http://www.ebi.ac.uk/pdbsum/1jbq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jbq RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==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. | 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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| - | ==Disease== | ||
| - | Known diseases associated with this structure: Homocystinuria, B6-responsive and nonresponsive types OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=236200 236200]], Thrombosis, hyperhomocysteinemic OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=236200 236200]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Kraus, J P.]] | [[Category: Kraus, J P.]] | ||
[[Category: Meier, M.]] | [[Category: Meier, M.]] | ||
| - | [[Category: HEM]] | ||
| - | [[Category: PLP]] | ||
[[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 Sun Mar | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:31:21 2008'' |
Revision as of 18:31, 30 March 2008
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| , resolution 2.60Å | |||||||
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| Ligands: | , | ||||||
| Activity: | Cystathionine beta-synthase, with EC number 4.2.1.22 | ||||||
| Related: | 1D6S
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF HUMAN CYSTATHIONINE BETA-SYNTHASE: A UNIQUE PYRIDOXAL 5'-PHOSPHATE DEPENDENT HEMEPROTEIN
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.
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
Page seeded by OCA on Sun Mar 30 21:31:21 2008
