4BPC

Structure of the Catalytic Domain of Protein Tyrosine Phosphatase Sigma in the Sulfenic Acid Form

Summary for 4BPC

• Entry DOI: 10.2210/pdb4bpc/pdb
• Descriptor: RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE S (2 entities in total)
• Functional Keywords: hydrolase, proteoglycan, redox regulation
• Biological source: HOMO SAPIENS (HUMAN)
• Total number of polymer chains: 1
• Total formula weight: 66932.55

Authors

Jeon, T.J.,Chien, P.N.,Chun, H.J.,Ryu, S.E. (deposition date: 2013-05-24, release date: 2013-07-17, Last modification date: 2024-10-16)

Primary citation

Jeon, T.J.,Chien, P.N.,Chun, H.J.,Ryu, S.E.
Structure of the Catalytic Domain of Protein Tyrosine Phosphatase Sigma in the Sulfenic Acid Form
Mol.Cells, 36:55-, 2013

PubMed Abstract: Protein tyrosine phosphatase sigma (PTPσ) plays a vital role in neural development. The extracellular domain of PTPσ binds to various proteoglycans, which control the activity of 2 intracellular PTP domains (D1 and D2). To understand the regulatory mechanism of PTPσ, we carried out structural and biochemical analyses of PTPσ D1D2. In the crystal structure analysis of a mutant form of D1D2 of PTPσ, we unexpectedly found that the catalytic cysteine of D1 is oxidized to cysteine sulfenic acid, while that of D2 remained in its reduced form, suggesting that D1 is more sensitive to oxidation than D2. This finding contrasts previous observations on PTPα. The cysteine sulfenic acid of D1 was further confirmed by immunoblot and mass spectrometric analyses. The stabilization of the cysteine sulfenic acid in the active site of PTP suggests that the formation of cysteine sulfenic acid may function as a stable intermediate during the redox-regulation of PTPs.

PubMed: 23820885
DOI: 10.1007/S10059-013-0033-X

Experimental method

X-RAY DIFFRACTION (2.1 Å)