title: Crystal structure of SP-PTP, a low molecular weight protein tyrosine phosphatase from Streptococcus pyogenes.
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.
authors.affiliation: Disease Target Structure Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon, Republic of Korea; Department of Bio-Analytical Science, University of Science and Technology, Daejeon, Republic of Korea. Electronic address: bku@kribb.re.kr.
authors.forename: Bonsu
authors.initials: B
authors.lastname: Ku
authors.affiliation: Disease Target Structure Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon, Republic of Korea; Department of Bio-Analytical Science, University of Science and Technology, Daejeon, Republic of Korea.
authors.forename: Chae Won
authors.initials: CW
authors.lastname: Keum
authors.affiliation: Disease Target Structure Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon, Republic of Korea; Department of Biology, Chungnam National University, Daejeon, Republic of Korea.
authors.forename: Hye Seon
authors.initials: HS
authors.lastname: Lee
authors.affiliation: Disease Target Structure Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon, Republic of Korea; Department of Bio-Analytical Science, University of Science and Technology, Daejeon, Republic of Korea.
authors.forename: Hye-Yeoung
authors.initials: HY
authors.lastname: Yun
authors.affiliation: Disease Target Structure Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon, Republic of Korea.
authors.forename: Ho-Chul
authors.initials: HC
authors.lastname: Shin
authors.affiliation: Incurable Diseases Therapeutics Research Center, World Class Institute, Korea Research Institute of Bioscience and Biotechnology, Ochang, Cheongwon, Republic of Korea.
authors.forename: Bo Yeon
authors.initials: BY
authors.lastname: Kim
authors.affiliation: Disease Target Structure Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon, Republic of Korea; Department of Bio-Analytical Science, University of Science and Technology, Daejeon, Republic of Korea. Electronic address: ksj@kribb.re.kr.
authors.forename: Seung Jun
authors.initials: SJ
authors.lastname: Kim
mesh_terms: D018360:Crystallography, X-Ray; D008958:Models, Molecular; D008970:Molecular Weight; D010766:Phosphorylation; D017433:Protein Structure, Secondary; D017027:Protein Tyrosine Phosphatases / Q000737:chemistry* / Q000378:metabolism; D013297:Streptococcus pyogenes / Q000201:enzymology*; D013379:Substrate Specificity
chemical_list: D017027:Protein Tyrosine Phosphatases
keywords: GAS; LMWPTP; Protein tyrosine phosphatase; Streptococcus pyogenes; Structure