3C7T

Crystal structure of the ecdysone phosphate phosphatase, EPPase, from Bombix mori in complex with tungstate

Summary for 3C7T

• Entry DOI: 10.2210/pdb3c7t/pdb
• Descriptor: Ecdysteroid-phosphate phosphatase, TUNGSTATE(VI)ION, CHLORIDE ION, ... (7 entities in total)
• Functional Keywords: phosphatase, ecdysone, 2h-phosphatase, pgm, hydrolase
• Biological source: Bombyx mori (Silk moth)
• Total number of polymer chains: 4
• Total formula weight: 120612.47

Authors

Chen, Y.,Carpino, N.,Nassar, N. (deposition date: 2008-02-08, release date: 2009-03-24, Last modification date: 2024-02-21)

Primary citation

Chen, Y.,Jakoncic, J.,Wang, J.,Zheng, X.,Carpino, N.,Nassar, N.
Structural and functional characterization of the c-terminal domain of the ecdysteroid phosphate phosphatase from Bombyx mori reveals a new enzymatic activity.
Biochemistry, 47:12135-12145, 2008

PubMed Abstract: Here, we present the crystal structure of the ecdysone phosphate phosphatase (EPPase) phosphoglycerate mutase (PGM) homology domain, the first structure of a steroid phosphate phosphatase. The structure reveals an alpha/beta-fold common to members of the two histidine (2H)-phosphatase superfamily with strong homology to the Suppressor of T-cell receptor signaling-1 (Sts-1 PGM) protein. The putative EPPase PGM active site contains signature residues shared by 2H-phosphatase enzymes, including a conserved histidine (His80) that acts as a nucleophile during catalysis. The physiological substrate ecdysone 22-phosphate was modeled in a hydrophobic cavity close to the phosphate-binding site. EPPase PGM shows limited substrate specificity with an ability to hydrolyze steroid phosphates, the phospho-tyrosine (pTyr) substrate analogue para-nitrophenylphosphate ( pNPP) and pTyr-containing peptides and proteins. Altogether, our data demonstrate a new protein tyrosine phosphatase (PTP) activity for EPPase. They suggest that EPPase and its closest homologues can be grouped into a distinct subfamily in the large 2H-phosphatase superfamily of proteins.

PubMed: 18937503
DOI: 10.1021/bi801318w

Experimental method

X-RAY DIFFRACTION (1.76 Å)