1q22
From Proteopedia
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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 NA, A3P and 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
Page seeded by OCA on Mon Nov 12 18:49:43 2007
Categories: Homo sapiens | Single protein | Fuda, H. | Lee, K.A. | Lee, Y.C. | Negishi, M. | Pedersen, L.C. | Strott, C.A. | A3P | AND | NA | Dhea | Pap | Sulfotransferase | Sult2b1b
