| No. Registro | 002468102 |
| Tipo de material | ARTIGO DE PERIODICO - INTERNACIONAL |
| Cód. publicação |  10.1107/S0907444913021550 DOI |
| Entrada Principal | Begum, Afshan (*) INT |
| Título | Staphylococcus 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 | PARASITOLOGIA |
| Autor Secundário | Drebes, Julia (*) University of Hamburg, Laboratory for Structural Biology of Infection and Inflammation, Hamburg, Germany INT |
| | Kikhney, Alexey (*) Europäisches Laboratorium für Molekularbiologie (EMBL), Hamburg, Germany INT |
| | Müller, Ingrid B. (*) Bernhard Nocht Institute for Tropical Medicine, Department of Biochemistry, Hamburg, Germany INT |
| | Perbandt, Markus (*) University of Hamburg, Laboratory for Structural Biology of Infection and Inflammation, Hamburg, Germany INT |
| | Svergun, Dmitri (*) Europäisches Laboratorium für Molekularbiologie (EMBL), Hamburg, Germany INT |
| | Wrenger, Carsten |
| | Betzel, Christian (*) University of Hamburg, Laboratory for Structural Biology of Infection and Inflammation, Hamburg, Germany INT |
| Fonte | In: Acta Crystallographica Section D, Biological Crystallography, Copenhagen, v. 69, pt. 12, p. 2320-2329, 2013, ISSN: 1399-0047 |
| Localiz.Eletrônica |
 "Clicar" sobre o botão para acesso ao texto completo |
| |
"Clicar" sobre o botão para acesso ao Currículo Lattes de Carsten Wrenger |
| 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 |
| |
|
| Acervo Geral | Todos os itens |
| Itens na Biblioteca | ICB-Inst. Ciências Biomédica |
| Unidade USP | ICB -- INST DE CIÊNCIAS BIOMÉDICAS |
