5GOT

Crystal structure of SP-PTP, low molecular weight protein tyrosine phosphatase from Streptococcus pyogenes

Summary for 5GOT

• Entry DOI: 10.2210/pdb5got/pdb
• Descriptor: Low molecular weight phosphotyrosine phosphatase family protein, CHLORIDE ION (3 entities in total)
• Functional Keywords: sp-ptp, lmwptp, streptococcus pyogenes, hydrolase
• Biological source: Streptococcus pyogenes
• Total number of polymer chains: 1
• Total formula weight: 18148.84

Authors

Ku, B.,Keum, C.W.,KIim, S.J. (deposition date: 2016-07-29, release date: 2016-09-07, Last modification date: 2024-03-20)

Primary citation

Ku, B.,Keum, C.W.,Lee, H.S.,Yun, H.-Y.,Shin, H.-C.,Kim, B.Y.,Kim, S.J.
Crystal structure of SP-PTP, a low molecular weight protein tyrosine phosphatase from Streptococcus pyogenes
Biochem.Biophys.Res.Commun., 478:1217-1222, 2016

PubMed Abstract: Streptococcus pyogenes, or Group A Streptococcus (GAS), is a pathogenic bacterium that causes a variety of infectious diseases. The GAS genome encodes one protein tyrosine phosphatase, SP-PTP, which plays an essential role in the replication and virulence maintenance of GAS. Herein, we present the crystal structure of SP-PTP at 1.9 Å resolution. Although SP-PTP has been reported to have dual phosphatase specificity for both phosphorylated tyrosine and serine/threonine, three-dimensional structural analysis showed that SP-PTP shares high similarity with typical low molecular weight protein tyrosine phosphatases (LMWPTPs), which are specific for phosphotyrosine, but not with dual-specificity phosphatases, in overall folding and active site composition. In the dephosphorylation activity test, SP-PTP consistently acted on phosphotyrosine substrates, but not or only minimally on phosphoserine/phosphothreonine substrates. Collectively, our structural and biochemical analyses verified SP-PTP as a canonical tyrosine-specific LMWPTP.

PubMed: 27545603
DOI: 10.1016/j.bbrc.2016.08.097

Experimental method

X-RAY DIFFRACTION (1.902 Å)