1cjm
From Proteopedia
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|PDB= 1cjm |SIZE=350|CAPTION= <scene name='initialview01'>1cjm</scene>, resolution 2.40Å | |PDB= 1cjm |SIZE=350|CAPTION= <scene name='initialview01'>1cjm</scene>, resolution 2.40Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cjm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cjm OCA], [http://www.ebi.ac.uk/pdbsum/1cjm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1cjm RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==Overview== | ||
Sulfonation, like phosphorylation, can modify the activity of a variety of biological molecules. The sulfotransferase enzymes sulfonate neurotransmitters, drugs, steroid hormones, dietary carcinogens and proteins. SULT1A3 specifically sulfonates catecholamines such as dopamine, adrenaline and noradrenaline. The crystal structure of SULT1A3 with a sulfate bound at the active site, has been determined at 2.4 A resolution. Although the core alpha/beta fold is like that of estrogen and heparan sulfotransferases, major differences occur in and around the active site. Most notably, several regions surrounding the active site, including a section of 40 residues, are disordered in SULT1A3. Regions that are topologically equivalent to the disordered parts of SULT1A3 are involved in substrate and cofactor binding in estrogen and heparan sulfotransferase. Flexibility in these regions suggests that ligand binding elicits a disorder-order transition in and around the active site of sulfotransferases and might contribute to the broad substrate specificity of these enzymes. | Sulfonation, like phosphorylation, can modify the activity of a variety of biological molecules. The sulfotransferase enzymes sulfonate neurotransmitters, drugs, steroid hormones, dietary carcinogens and proteins. SULT1A3 specifically sulfonates catecholamines such as dopamine, adrenaline and noradrenaline. The crystal structure of SULT1A3 with a sulfate bound at the active site, has been determined at 2.4 A resolution. Although the core alpha/beta fold is like that of estrogen and heparan sulfotransferases, major differences occur in and around the active site. Most notably, several regions surrounding the active site, including a section of 40 residues, are disordered in SULT1A3. Regions that are topologically equivalent to the disordered parts of SULT1A3 are involved in substrate and cofactor binding in estrogen and heparan sulfotransferase. Flexibility in these regions suggests that ligand binding elicits a disorder-order transition in and around the active site of sulfotransferases and might contribute to the broad substrate specificity of these enzymes. | ||
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| - | ==Disease== | ||
| - | Known diseases associated with this structure: Alzheimer disease-4 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=600759 600759]], Cardiomyopathy, dilated, 1V OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=600759 600759]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Negishi, M.]] | [[Category: Negishi, M.]] | ||
[[Category: Pedersen, L.]] | [[Category: Pedersen, L.]] | ||
| - | [[Category: SO4]] | ||
[[Category: dopamine]] | [[Category: dopamine]] | ||
[[Category: hast3]] | [[Category: hast3]] | ||
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[[Category: sult1a3]] | [[Category: sult1a3]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:23:00 2008'' |
Revision as of 16:23, 30 March 2008
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| , resolution 2.40Å | |||||||
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
HUMAN SULT1A3 WITH SULFATE BOUND
Overview
Sulfonation, like phosphorylation, can modify the activity of a variety of biological molecules. The sulfotransferase enzymes sulfonate neurotransmitters, drugs, steroid hormones, dietary carcinogens and proteins. SULT1A3 specifically sulfonates catecholamines such as dopamine, adrenaline and noradrenaline. The crystal structure of SULT1A3 with a sulfate bound at the active site, has been determined at 2.4 A resolution. Although the core alpha/beta fold is like that of estrogen and heparan sulfotransferases, major differences occur in and around the active site. Most notably, several regions surrounding the active site, including a section of 40 residues, are disordered in SULT1A3. Regions that are topologically equivalent to the disordered parts of SULT1A3 are involved in substrate and cofactor binding in estrogen and heparan sulfotransferase. Flexibility in these regions suggests that ligand binding elicits a disorder-order transition in and around the active site of sulfotransferases and might contribute to the broad substrate specificity of these enzymes.
About this Structure
1CJM is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of human catecholamine sulfotransferase., Bidwell LM, McManus ME, Gaedigk A, Kakuta Y, Negishi M, Pedersen L, Martin JL, J Mol Biol. 1999 Oct 29;293(3):521-30. PMID:10543947
Page seeded by OCA on Sun Mar 30 19:23:00 2008
Categories: Homo sapiens | Single protein | Bidwell, L M. | Gaedigk, A. | Kakuta, Y. | Martin, J L. | Mcmanus, M E. | Negishi, M. | Pedersen, L. | Dopamine | Hast3 | Pap | Sulfotransferase | Sult1a3
