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Dynamic cross correlation analysis of Thermus thermophilus alkaline phosphatase and determinants of thermostability.
Borges, Bruno; Gallo, Gloria; Coelho, Camila; Negri, Naiane; Maiello, Fernando; Hardy, Leon; Würtele, Martin.
Afiliação
  • Borges B; Department of Science and Technology, Federal University of São Paulo, São José dos Campos, Brazil.
  • Gallo G; Department of Science and Technology, Federal University of São Paulo, São José dos Campos, Brazil.
  • Coelho C; Department of Science and Technology, Federal University of São Paulo, São José dos Campos, Brazil.
  • Negri N; Department of Science and Technology, Federal University of São Paulo, São José dos Campos, Brazil; Alberto Luiz Coimbra Institute for Graduate Studies and Research in Engineering (COPPE), Federal University of Rio de Janeiro, Rio de Janeiro, Brazil.
  • Maiello F; Department of Science and Technology, Federal University of São Paulo, São José dos Campos, Brazil.
  • Hardy L; Department of Physics, University of South Florida, Tampa, United States.
  • Würtele M; Department of Science and Technology, Federal University of São Paulo, São José dos Campos, Brazil. Electronic address: martin.wurtele@unifesp.br.
Biochim Biophys Acta Gen Subj ; 1865(7): 129895, 2021 07.
Article em En | MEDLINE | ID: mdl-33781823
BACKGROUND: Understanding the determinants of protein thermostability is very important both from the theoretical and applied perspective. One emerging view in thermostable enzymes seems to indicate that a salt bridge/charged residue network plays a fundamental role in their thermostability. METHODS: The structure of alkaline phosphatase (AP) from Thermus thermophilus HB8 was solved by X-ray crystallography at 2.1 Å resolution. The obtained structure was further analyzed by molecular dynamics studies at different temperatures (303 K, 333 K and 363 K) and compared to homologous proteins from the cold-adapted organisms Shewanella sp. and Vibrio strain G15-21. To analyze differences in measures of dynamic variation, several data reduction techniques like principal component analysis (PCA), residue interaction network (RIN) analysis and rotamer analysis were used. Using hierarchical clustering, the obtained results were combined to determine residues showing high degree dynamical variations due to temperature jumps. Furthermore, dynamic cross correlation (DCC) analysis was carried out to characterize networks of charged residues. RESULTS: Top clustered residues showed a higher propensity for thermostabilizing mutations, indicating evolutionary pressure acting on thermophilic organisms. The description of rotamer distributions by Gini coefficients and Kullback-Leibler (KL) divergence both revealed significant correlations with temperature. DCC analysis revealed a significant trend to de-correlation of the movement of charged residues at higher temperatures. SIGNIFICANCE: The de-correlation of charged residues detected in Thermus thermophilus AP, highlights the importance of dynamic electrostatic network interactions for the thermostability of this enzyme.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Thermus thermophilus / Fosfatase Alcalina / Temperatura Alta Idioma: En Revista: Biochim Biophys Acta Gen Subj Ano de publicação: 2021 Tipo de documento: Article País de afiliação: Brasil País de publicação: Holanda
Texto completo
Adicionar na Minha BVS
Imprimir
XML
PubMed Links
Buscar no Google

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Thermus thermophilus / Fosfatase Alcalina / Temperatura Alta Idioma: En Revista: Biochim Biophys Acta Gen Subj Ano de publicação: 2021 Tipo de documento: Article País de afiliação: Brasil País de publicação: Holanda