1hy3: Difference between revisions
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[[Image:1hy3.gif|left|200px]] | [[Image:1hy3.gif|left|200px]] | ||
'''CRYSTAL STRUCTURE OF HUMAN ESTROGEN SULFOTRANSFERASE V269E MUTANT IN THE PRESENCE OF PAPS''' | {{Structure | ||
|PDB= 1hy3 |SIZE=350|CAPTION= <scene name='initialview01'>1hy3</scene>, resolution 1.80Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=PPS:3'-PHOSPHATE-ADENOSINE-5'-PHOSPHATE SULFATE'>PPS</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Estrone_sulfotransferase Estrone sulfotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.8.2.4 2.8.2.4] | |||
|GENE= STE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |||
}} | |||
'''CRYSTAL STRUCTURE OF HUMAN ESTROGEN SULFOTRANSFERASE V269E MUTANT IN THE PRESENCE OF PAPS''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1HY3 is a [ | 1HY3 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=1HY3 OCA]. | ||
==Reference== | ==Reference== | ||
Crystal structure of the human estrogen sulfotransferase-PAPS complex: evidence for catalytic role of Ser137 in the sulfuryl transfer reaction., Pedersen LC, Petrotchenko E, Shevtsov S, Negishi M, J Biol Chem. 2002 May 17;277(20):17928-32. Epub 2002 Mar 7. PMID:[http:// | Crystal structure of the human estrogen sulfotransferase-PAPS complex: evidence for catalytic role of Ser137 in the sulfuryl transfer reaction., Pedersen LC, Petrotchenko E, Shevtsov S, Negishi M, J Biol Chem. 2002 May 17;277(20):17928-32. Epub 2002 Mar 7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11884392 11884392] | ||
[[Category: Estrone sulfotransferase]] | [[Category: Estrone sulfotransferase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
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[[Category: estrogen]] | [[Category: estrogen]] | ||
[[Category: human]] | [[Category: human]] | ||
[[Category: | [[Category: pap]] | ||
[[Category: sulfotransferase]] | [[Category: sulfotransferase]] | ||
''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 11:43:00 2008'' | ||
Revision as of 12:43, 20 March 2008
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| , resolution 1.80Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | STE (Homo sapiens) | ||||||
| Activity: | Estrone sulfotransferase, with EC number 2.8.2.4 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF HUMAN ESTROGEN SULFOTRANSFERASE V269E MUTANT IN THE PRESENCE OF PAPS
OverviewOverview
Estrogen sulfotransferase (EST) transfers the sulfate group from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to estrogenic steroids. Here we report the crystal structure of human EST (hEST) in the context of the V269E mutant-PAPS complex, which is the first structure containing the active sulfate donor for any sulfotransferase. Superimposing this structure with the crystal structure of hEST in complex with the donor product 3'-phosphoadenosine 5'-phosphate (PAP) and the acceptor substrate 17beta-estradiol, the ternary structure with the PAPS and estradiol molecule, is modeled. These structures have now provided a more complete view of the S(N)2-like in-line displacement reaction catalyzed by sulfotransferases. In the PAPS-bound structure, the side chain nitrogen of the catalytic Lys(47) interacts with the side chain hydroxyl of Ser(137) and not with the bridging oxygen between the 5'-phosphate and sulfate groups of the PAPS molecule as is seen in the PAP-bound structures. This conformational change of the side chain nitrogen indicates that the interaction of Lys(47) with Ser(137) may regulate PAPS hydrolysis in the absences of an acceptor substrate. Supporting the structural data, the mutations of Ser(137) to cysteine and alanine decrease gradually k(cat) for PAPS hydrolysis and transfer activity. Thus, Ser(137) appears to play an important role in regulating the side chain interaction of Lys(47) with the bridging oxygen between the 5'-phosphate and the sulfate of PAPS.
DiseaseDisease
Known diseases associated with this structure: Mandibuloacral dysplasia with type B lipodystrophy OMIM:[606480], Restrictive dermopathy, lethal OMIM:[606480]
About this StructureAbout this Structure
1HY3 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the human estrogen sulfotransferase-PAPS complex: evidence for catalytic role of Ser137 in the sulfuryl transfer reaction., Pedersen LC, Petrotchenko E, Shevtsov S, Negishi M, J Biol Chem. 2002 May 17;277(20):17928-32. Epub 2002 Mar 7. PMID:11884392
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