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Arch Biochem Biophys ; 681: 108277, 2020 03 15.
Artigo em Inglês | MEDLINE | ID: mdl-31978399

RESUMO

Low molecular weight protein tyrosine phosphatases (LMW-PTP) are ubiquitous enzymes found across a spectrum of genera from prokaryotes to higher eukaryotes. LMW-PTP belong to the Cys-based PTP class II protein family. Here, we show that LMW-PTP can be categorized into two different groups, referred as class II subdivision I (class II.I) and subdivision II (class II.II). Using BPtpA from the opportunistic pathogen Burkholderia cenocepacia, as a representative member of the LMW-PTP class II.I, we demonstrated that four conserved residues (W47, H48, D80, and F81) are required for enzyme function. Guided by an in silico model of BPtpA, we show that the conserved residues at α3-helix (D80 and F81) contribute to protein stability, while the other conserved residues in the W-loop (W47 and H48) likely play a role in substrate recognition. Overall, our results provide new information on LMW-PTP protein family and establish B. cenocepacia as a suitable model to investigate how substrates are recognized and sorted by these proteins.


Assuntos
Proteínas de Bactérias/metabolismo , Burkholderia cenocepacia/metabolismo , Proteínas Tirosina Fosfatases/metabolismo , Sequência de Aminoácidos , Proteínas de Bactérias/química , Infecções por Burkholderia/microbiologia , Burkholderia cenocepacia/química , Humanos , Modelos Moleculares , Fosforilação , Proteínas Tirosina Fosfatases/química
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