6APX

Crystal structure of human dual specificity phosphatase 1 catalytic domain (C258S) as a maltose binding protein fusion in complex with the monobody YSX1

Summary for 6APX

• Entry DOI: 10.2210/pdb6apx/pdb
• Descriptor: Maltose-binding periplasmic protein,Dual specificity protein phosphatase 1, Monobody YSX1, SULFATE ION, ... (5 entities in total)
• Functional Keywords: dual specificity phosphatase, dusp, c258s, hydrolase
• Biological source: Escherichia coli (strain K12); More
• Cellular location: Nucleus : P28562
• Total number of polymer chains: 2
• Total formula weight: 67899.48

Authors

Gumpena, R.,Lountos, G.T.,Sreejith, R.K.,Tropea, J.E.,Cherry, S.,Waugh, D.S. (deposition date: 2017-08-18, release date: 2017-11-01, Last modification date: 2023-10-04)

Primary citation

Gumpena, R.,Lountos, G.T.,Raran-Kurussi, S.,Tropea, J.E.,Cherry, S.,Waugh, D.S.
Crystal structure of the human dual specificity phosphatase 1 catalytic domain.
Protein Sci., 27:561-567, 2018

PubMed Abstract: The dual specificity phosphatase DUSP1 was the first mitogen activated protein kinase phosphatase (MKP) to be identified. It dephosphorylates conserved tyrosine and threonine residues in the activation loops of mitogen activated protein kinases ERK2, JNK1 and p38-alpha. Here, we report the crystal structure of the human DUSP1 catalytic domain at 2.49 Å resolution. Uniquely, the protein was crystallized as an MBP fusion protein in complex with a monobody that binds to MBP. Sulfate ions occupy the phosphotyrosine and putative phosphothreonine binding sites in the DUSP1 catalytic domain.

PubMed: 29052270
DOI: 10.1002/pro.3328

Experimental method

X-RAY DIFFRACTION (2.491 Å)