1fw1
From Proteopedia
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| - | [[Image:1fw1.jpg|left|200px]] | + | [[Image:1fw1.jpg|left|200px]] |
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| - | '''GLUTATHIONE TRANSFERASE ZETA/MALEYLACETOACETATE ISOMERASE''' | + | {{Structure |
| + | |PDB= 1fw1 |SIZE=350|CAPTION= <scene name='initialview01'>1fw1</scene>, resolution 1.90Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=DTT:2,3-DIHYDROXY-1,4-DITHIOBUTANE'>DTT</scene> and <scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''GLUTATHIONE TRANSFERASE ZETA/MALEYLACETOACETATE ISOMERASE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1FW1 is a [ | + | 1FW1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FW1 OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure of maleylacetoacetate isomerase/glutathione transferase zeta reveals the molecular basis for its remarkable catalytic promiscuity., Polekhina G, Board PG, Blackburn AC, Parker MW, Biochemistry. 2001 Feb 13;40(6):1567-76. PMID:[http:// | + | Crystal structure of maleylacetoacetate isomerase/glutathione transferase zeta reveals the molecular basis for its remarkable catalytic promiscuity., Polekhina G, Board PG, Blackburn AC, Parker MW, Biochemistry. 2001 Feb 13;40(6):1567-76. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11327815 11327815] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: glutathione transferase]] | [[Category: glutathione transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:14:46 2008'' |
Revision as of 09:14, 20 March 2008
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| , resolution 1.90Å | |||||||
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| Ligands: | , and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
GLUTATHIONE TRANSFERASE ZETA/MALEYLACETOACETATE ISOMERASE
Contents |
Overview
Maleylacetoacetate isomerase (MAAI), a key enzyme in the metabolic degradation of phenylalanine and tyrosine, catalyzes the glutathione-dependent isomerization of maleylacetoacetate to fumarylacetoacetate. Deficiencies in enzymes along the degradation pathway lead to serious diseases including phenylketonuria, alkaptonuria, and the fatal disease, hereditary tyrosinemia type I. The structure of MAAI might prove useful in the design of inhibitors that could be used in the clinical management of the latter disease. Here we report the crystal structure of human MAAI at 1.9 A resolution in complex with glutathione and a sulfate ion which mimics substrate binding. The enzyme has previously been shown to belong to the zeta class of the glutathione S-transferase (GST) superfamily based on limited sequence similarity. The structure of MAAI shows that it does adopt the GST canonical fold but with a number of functionally important differences. The structure provides insights into the molecular bases of the remarkable array of different reactions the enzyme is capable of performing including isomerization, oxygenation, dehalogenation, peroxidation, and transferase activity.
Disease
Known diseases associated with this structure: Tyrosinemia, type Ib OMIM:[603758]
About this Structure
1FW1 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of maleylacetoacetate isomerase/glutathione transferase zeta reveals the molecular basis for its remarkable catalytic promiscuity., Polekhina G, Board PG, Blackburn AC, Parker MW, Biochemistry. 2001 Feb 13;40(6):1567-76. PMID:11327815
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