5WRJ

Crystal structure of human tyrosylprotein sulfotransferase-1 complexed with PAP and gastrin peptide

Summary for 5WRJ

• Entry DOI: 10.2210/pdb5wrj/pdb
• Related: 3AP1 5WRI
• Descriptor: Protein-tyrosine sulfotransferase 1, gastrin peptide, ADENOSINE-3'-5'-DIPHOSPHATE, ... (5 entities in total)
• Functional Keywords: transferase
• Biological source: Homo sapiens (Human); More
• Cellular location: Golgi apparatus membrane ; Single-pass type II membrane protein : O60507
• Total number of polymer chains: 8
• Total formula weight: 145437.29

Authors

Tanaka, S.,Nishiyori, T.,Kojo, H.,Otsubo, R.,Kakuta, Y. (deposition date: 2016-12-02, release date: 2017-09-06, Last modification date: 2024-11-13)

Primary citation

Tanaka, S.,Nishiyori, T.,Kojo, H.,Otsubo, R.,Tsuruta, M.,Kurogi, K.,Liu, M.C.,Suiko, M.,Sakakibara, Y.,Kakuta, Y.
Structural basis for the broad substrate specificity of the human tyrosylprotein sulfotransferase-1.
Sci Rep, 7:8776-8776, 2017

PubMed Abstract: Tyrosylprotein sulfotransferases (TPSTs) are enzymes that catalyze post-translational tyrosine sulfation of proteins. In humans, there are only two TPST isoforms, designated TPST1 and TPST2. In a previous study, we reported the crystal structure of TPST2, which revealed the catalytic mechanism of the tyrosine sulfation reaction. However, detailed molecular mechanisms underlying how TPSTs catalyse a variety of substrate proteins with different efficiencies and how TPSTs catalyze the sulfation of multiple tyrosine residues in a substrate protein remain unresolved. Here, we report two crystal structures of the human TPST1 complexed with two substrate peptides that are catalysed by human TPST1 with significantly different efficiencies. The distinct binding modes found in the two complexes provide insight into the sulfation mechanism for these substrates. The present study provides valuable information describing the molecular mechanism of post-translational protein modifications catalysed by TPSTs.

PubMed: 28821720
DOI: 10.1038/s41598-017-07141-8

Experimental method

X-RAY DIFFRACTION (2.31 Å)