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Escolher formato: Padrão Ficha Formato Reduzido Nomes MARC Campos MARC
No. Registro   002468102
Tipo de material   ARTIGO DE PERIODICO - INTERNACIONAL
Cód. publicação   Link10.1107/S0907444913021550 DOI
Entrada Principal   LinkBegum, Afshan (*) INT
Título   LinkStaphylococcus aureus thiaminase II : oligomerization warrants proteolytic protection against serine proteases.
Imprenta   Copenhagen, 2013.
Descrição   p. 2320-2329.
Idioma   Inglês
Nota   Disponível em: <http://dx.doi.org/10.1107/S0907444913021550>. Acesso em: 20 jan. 2014
Assunto   LinkPARASITOLOGIA
Autor Secundário   LinkDrebes, Julia (*) University of Hamburg, Laboratory for Structural Biology of Infection and Inflammation, Hamburg, Germany INT
  LinkKikhney, Alexey (*) Europäisches Laboratorium für Molekularbiologie (EMBL), Hamburg, Germany INT
  LinkMüller, Ingrid B. (*) Bernhard Nocht Institute for Tropical Medicine, Department of Biochemistry, Hamburg, Germany INT
  LinkPerbandt, Markus (*) University of Hamburg, Laboratory for Structural Biology of Infection and Inflammation, Hamburg, Germany INT
  LinkSvergun, Dmitri (*) Europäisches Laboratorium für Molekularbiologie (EMBL), Hamburg, Germany INT
  LinkWrenger, Carsten
  LinkBetzel, Christian (*) University of Hamburg, Laboratory for Structural Biology of Infection and Inflammation, Hamburg, Germany INT
Fonte   LinkIn: Acta Crystallographica Section D, Biological Crystallography, Copenhagen, v. 69, pt. 12, p. 2320-2329, 2013, ISSN: 1399-0047
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Resumo/Outros   Staphylococcus aureus TenA (SaTenA) is a thiaminase type II enzyme that catalyzes the deamination of aminopyrimidine, as well as the cleavage of thiamine into 4-amino-5-hydroxymethyl- 2-methylpyrimidine (HMP) and 5-(2-hydroxyethyl)- 4-methylthiazole (THZ), within thiamine (vitamin B1) metabolism. Further, by analogy with studies of Bacillus subtilis TenA, SaTenA may act as a regulator controlling the secretion of extracellular proteases such as the subtilisin type of enzymes in bacteria. Thiamine biosynthesis has been identified as a potential drug target of the multi-resistant pathogen S. aureus and therefore all enzymes involved in the S. aureus thiamine pathway are presently being investigated in detail. Here, the structure of SaTenA, determined by molecular replacement and refined at 2.7 Å resolution to an R factor of 21.6% with one homotetramer in the asymmetric unit in the orthorhombic space group P212121, is presented. The tetrameric state of wild-type (WT) SaTenA was postulated to be the functional biological unit and was confirmed by small-angle X-ray scattering (SAXS) experiments in solution. To obtain insights into structural and functional features of the oligomeric SaTenA, comparative kinetic investigations as well as experiments analyzing the structural stability of the WT SaTenA tetramer versus a monomeric SaTenA mutant were performed
 
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Escolher formato: Padrão Ficha Formato Reduzido Nomes MARC Campos MARC


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