2ZVP

Crystal structure of mouse cytosolic sulfotransferase mSULT1D1 complex with PAP and p-nitrophenol

Summary for 2ZVP

• Entry DOI: 10.2210/pdb2zvp/pdb
• Related: 2ZPT 2ZVQ
• Descriptor: Tyrosine-ester sulfotransferase, ADENOSINE-3'-5'-DIPHOSPHATE, P-NITROPHENOL, ... (5 entities in total)
• Functional Keywords: sult1d1, sulfotransferase, p-nitrophenol, sulfonation, transferase
• Biological source: Mus musculus (mouse)
• Total number of polymer chains: 1
• Total formula weight: 35925.81

Authors

Teramoto, T.,Sakakibara, Y.,Liu, M.-C.,Suiko, M.,Kimura, M.,Kakuta, Y. (deposition date: 2008-11-14, release date: 2008-12-30, Last modification date: 2023-11-01)

Primary citation

Teramoto, T.,Sakakibara, Y.,Liu, M.-C.,Suiko, M.,Kimura, M.,Kakuta, Y.
Structural basis for the broad range substrate specificity of a novel mouse cytosolic sulfotransferase--mSULT1D1
Biochem.Biophys.Res.Commun., 379:76-80, 2009

PubMed Abstract: The mouse cytosolic sulfotransferase, mSULT1D1, catalyzes the sulfonation of a wide range of phenolic molecules including p-nitrophenol (pNP), alpha-naphthol (alphaNT), serotonin, as well as dopamine and its metabolites. To gain insight into the structural basis for its broad range substrate specificity, we solved two distinct ternary crystal structures of mSULT1D1, complexed with 3'-phosphoadenosine-5'-phosphate (PAP) plus pNP or PAP plus alphaNT. The structures revealed that the mSULT1D1 contains an L-shaped accepter-binding site which comprises 20 amino acid residues and four conserved water molecules. The shape of the accepter-binding site can be adjusted by conformational changes of two residues, Ile148 and Glu247, upon binding with respective substrates.

PubMed: 19073143
DOI: 10.1016/j.bbrc.2008.12.013

Experimental method

X-RAY DIFFRACTION (1.3 Å)