1cjm: Difference between revisions
New page: left|200px<br /> <applet load="1cjm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cjm, resolution 2.40Å" /> '''HUMAN SULT1A3 WITH ... |
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[[Image:1cjm.gif|left|200px]]<br /> | [[Image:1cjm.gif|left|200px]]<br /><applet load="1cjm" size="350" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="1cjm" size=" | |||
caption="1cjm, resolution 2.40Å" /> | caption="1cjm, resolution 2.40Å" /> | ||
'''HUMAN SULT1A3 WITH SULFATE BOUND'''<br /> | '''HUMAN SULT1A3 WITH SULFATE BOUND'''<br /> | ||
==Overview== | ==Overview== | ||
Sulfonation, like phosphorylation, can modify the activity of a variety of | 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. | ||
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
1CJM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 1CJM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CJM OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Bidwell, L | [[Category: Bidwell, L M.]] | ||
[[Category: Gaedigk, A.]] | [[Category: Gaedigk, A.]] | ||
[[Category: Kakuta, Y.]] | [[Category: Kakuta, Y.]] | ||
[[Category: Martin, J | [[Category: Martin, J L.]] | ||
[[Category: Mcmanus, M | [[Category: Mcmanus, M E.]] | ||
[[Category: Negishi, M.]] | [[Category: Negishi, M.]] | ||
[[Category: Pedersen, L.]] | [[Category: Pedersen, L.]] | ||
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[[Category: sult1a3]] | [[Category: sult1a3]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:06:43 2008'' | ||
Revision as of 13:06, 21 February 2008
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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 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
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