7CUY

Crystal structure of Primo-1

Summary for 7CUY

• Entry DOI: 10.2210/pdb7cuy/pdb
• Descriptor: Low molecular weight phosphotyrosine protein phosphatase 1, 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID (3 entities in total)
• Functional Keywords: lmw-ptp, lmwptp, primo-1, hydrolase
• Biological source: Drosophila melanogaster (Fruit fly)
• Total number of polymer chains: 2
• Total formula weight: 37783.70

Authors

Lee, H.S.,Kim, S.J.,Ku, B. (deposition date: 2020-08-25, release date: 2021-01-13, Last modification date: 2023-11-29)

Primary citation

Lee, H.S.,Mo, Y.,Shin, H.C.,Kim, S.J.,Ku, B.
Structural and Biochemical Characterization of the Two Drosophila Low Molecular Weight-Protein Tyrosine Phosphatases DARP and Primo-1.
Mol.Cells, 43:1035-1045, 2020

PubMed Abstract: The genome contains four low molecular weightprotein tyrosine phosphatase (LMW-PTP) members: Primo-1, Primo-2, CG14297, and CG31469. The lack of intensive biochemical analysis has limited our understanding of these proteins. Primo-1 and CG31469 were previously classified as pseudophosphatases, but CG31469 was also suggested to be a putative protein arginine phosphatase. Herein, we present the crystal structures of CG31469 and Primo-1, which are the first LMW-PTP structures. Structural analysis showed that the two proteins adopt the typical LMW-PTP fold and have a canonically arranged P-loop. Intriguingly, while Primo-1 is presumed to be a canonical LMW-PTP, CG31469 is unique as it contains a threonine residue at the fifth position of the P-loop motif instead of highly conserved isoleucine and a characteristically narrow active site pocket, which should facilitate the accommodation of phosphoarginine. Subsequent biochemical analysis revealed that Primo-1 and CG31469 are enzymatically active on phosphotyrosine and phosphoarginine, respectively, refuting their classification as pseudophosphatases. Collectively, we provide structural and biochemical data on two proteins: Primo-1, the canonical LMW-PTP protein, and CG31469, the first investigated eukaryotic protein arginine phosphatase. We named CG31469 as DARP, which stands for ARginine Phosphatase.

PubMed: 33372666
DOI: 10.14348/molcells.2020.0192

Experimental method

X-RAY DIFFRACTION (2.081 Å)