1q22

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(New page: 200px<br /> <applet load="1q22" size="450" color="white" frame="true" align="right" spinBox="true" caption="1q22, resolution 2.50&Aring;" /> '''Crystal structure o...)
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<applet load="1q22" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1q22, resolution 2.50&Aring;" />
caption="1q22, resolution 2.50&Aring;" />
'''Crystal structure of human cholesterol sulfotransferase (SULT2B1b) in the presence of DHEA and PAP'''<br />
'''Crystal structure of human cholesterol sulfotransferase (SULT2B1b) in the presence of DHEA and PAP'''<br />
==Overview==
==Overview==
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The gene for human hydroxysteroid sulfotransferase (SULT2B1) encodes two, peptides, SULT2B1a and SULT2B1b, that differ only at their amino termini., SULT2B1b has a predilection for cholesterol but is also capable of, sulfonating pregnenolone, whereas SULT2B1a preferentially sulfonates, pregnenolone and only minimally sulfonates cholesterol. We have determined, the crystal structure of SULT2B1a and SULT2B1b bound to the substrate, donor product 3'-phosphoadenosine 5'-phosphate at 2.9 and 2.4 A, respectively, as well as SULT2B1b in the presence of the acceptor, substrate pregnenolone at 2.3 A. These structures reveal a different, catalytic binding orientation for the substrate from a previously, determined structure of hydroxysteroid sulfotransferase (SULT2A1) binding, dehydroepiandrosterone. In addition, the amino-terminal helix comprising, residues Asp19 to Lys26, which determines the specificity difference, between the SULT2B1 isoforms, becomes ordered upon pregnenolone binding, covering the substrate binding pocket.
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The gene for human hydroxysteroid sulfotransferase (SULT2B1) encodes two peptides, SULT2B1a and SULT2B1b, that differ only at their amino termini. SULT2B1b has a predilection for cholesterol but is also capable of sulfonating pregnenolone, whereas SULT2B1a preferentially sulfonates pregnenolone and only minimally sulfonates cholesterol. We have determined the crystal structure of SULT2B1a and SULT2B1b bound to the substrate donor product 3'-phosphoadenosine 5'-phosphate at 2.9 and 2.4 A, respectively, as well as SULT2B1b in the presence of the acceptor substrate pregnenolone at 2.3 A. These structures reveal a different catalytic binding orientation for the substrate from a previously determined structure of hydroxysteroid sulfotransferase (SULT2A1) binding dehydroepiandrosterone. In addition, the amino-terminal helix comprising residues Asp19 to Lys26, which determines the specificity difference between the SULT2B1 isoforms, becomes ordered upon pregnenolone binding, covering the substrate binding pocket.
==About this Structure==
==About this Structure==
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1Q22 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 NA, A3P and AND as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Q22 OCA].
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1Q22 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=NA:'>NA</scene>, <scene name='pdbligand=A3P:'>A3P</scene> and <scene name='pdbligand=AND:'>AND</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q22 OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Fuda, H.]]
[[Category: Fuda, H.]]
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[[Category: Lee, K.A.]]
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[[Category: Lee, K A.]]
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[[Category: Lee, Y.C.]]
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[[Category: Lee, Y C.]]
[[Category: Negishi, M.]]
[[Category: Negishi, M.]]
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[[Category: Pedersen, L.C.]]
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[[Category: Pedersen, L C.]]
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[[Category: Strott, C.A.]]
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[[Category: Strott, C A.]]
[[Category: A3P]]
[[Category: A3P]]
[[Category: AND]]
[[Category: AND]]
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[[Category: sult2b1b]]
[[Category: sult2b1b]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:49:43 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:35:08 2008''

Revision as of 12:35, 21 February 2008


1q22, resolution 2.50Å

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Crystal structure of human cholesterol sulfotransferase (SULT2B1b) in the presence of DHEA and PAP

Overview

The gene for human hydroxysteroid sulfotransferase (SULT2B1) encodes two peptides, SULT2B1a and SULT2B1b, that differ only at their amino termini. SULT2B1b has a predilection for cholesterol but is also capable of sulfonating pregnenolone, whereas SULT2B1a preferentially sulfonates pregnenolone and only minimally sulfonates cholesterol. We have determined the crystal structure of SULT2B1a and SULT2B1b bound to the substrate donor product 3'-phosphoadenosine 5'-phosphate at 2.9 and 2.4 A, respectively, as well as SULT2B1b in the presence of the acceptor substrate pregnenolone at 2.3 A. These structures reveal a different catalytic binding orientation for the substrate from a previously determined structure of hydroxysteroid sulfotransferase (SULT2A1) binding dehydroepiandrosterone. In addition, the amino-terminal helix comprising residues Asp19 to Lys26, which determines the specificity difference between the SULT2B1 isoforms, becomes ordered upon pregnenolone binding, covering the substrate binding pocket.

About this Structure

1Q22 is a Single protein structure of sequence from Homo sapiens with , and as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of human cholesterol sulfotransferase (SULT2B1b) in the presence of pregnenolone and 3'-phosphoadenosine 5'-phosphate. Rationale for specificity differences between prototypical SULT2A1 and the SULT2BG1 isoforms., Lee KA, Fuda H, Lee YC, Negishi M, Strott CA, Pedersen LC, J Biol Chem. 2003 Nov 7;278(45):44593-9. Epub 2003 Aug 14. PMID:12923182

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