1cjm
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HUMAN SULT1A3 WITH SULFATE BOUND
OverviewOverview
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.
DiseaseDisease
Known diseases associated with this structure: Alzheimer disease-4 OMIM:[600759], Cardiomyopathy, dilated, 1V OMIM:[600759]
About this StructureAbout this Structure
1CJM is a Single protein structure of sequence from Homo sapiens with SO4 as ligand. Full crystallographic information is available from OCA.
ReferenceReference
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 Mon Nov 12 16:22:30 2007