[PMID]: | 26524597 |
[Au] Autor: | de la Peña AH; Suarez A; Duong-Ly KC; Schoeffield AJ; Pizarro-Dupuy MA; Zarr M; Pineiro SA; Amzel LM; Gabelli SB |
[Ad] Endereço: | Department of Biomedical Engineering, Johns Hopkins University School of Medicine, Baltimore, Maryland, United States of America; Structural Enzymology and Thermodynamics Group, Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, Maryland, Unit |
[Ti] Título: | Structural and Enzymatic Characterization of a Nucleoside Diphosphate Sugar Hydrolase from Bdellovibrio bacteriovorus. |
[So] Source: | PLoS One;10(11):e0141716, 2015. |
[Is] ISSN: | 1932-6203 |
[Cp] País de publicação: | United States |
[La] Idioma: | eng |
[Ab] Resumo: | Given the broad range of substrates hydrolyzed by Nudix (nucleoside diphosphate linked to X) enzymes, identification of sequence and structural elements that correctly predict a Nudix substrate or characterize a family is key to correctly annotate the myriad of Nudix enzymes. Here, we present the structure determination and characterization of Bd3179 -- a Nudix hydrolase from Bdellovibrio bacteriovorus-that we show localized in the periplasmic space of this obligate Gram-negative predator. We demonstrate that the enzyme is a nucleoside diphosphate sugar hydrolase (NDPSase) and has a high degree of sequence and structural similarity to a canonical ADP-ribose hydrolase and to a nucleoside diphosphate sugar hydrolase (1.4 and 1.3 Å Cα RMSD respectively). Examination of the structural elements conserved in both types of enzymes confirms that an aspartate-X-lysine motif on the C-terminal helix of the α-ß-α NDPSase fold differentiates NDPSases from ADPRases. |
[Mh] Termos MeSH primário: |
Proteínas de Bactérias/química Proteínas de Bactérias/metabolismo Bdellovibrio/enzimologia Pirofosfatases/química Pirofosfatases/metabolismo
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[Mh] Termos MeSH secundário: |
Proteínas de Bactérias/genética Bdellovibrio/genética Domínio Catalítico Clonagem Molecular Modelos Moleculares Açúcares de Nucleosídeo Difosfato/metabolismo Periplasma/metabolismo Estrutura Terciária de Proteína Pirofosfatases/genética Homologia de Sequência de Aminoácidos
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[Pt] Tipo de publicação: | JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S. |
[Nm] Nome de substância:
| 0 (Bacterial Proteins); 0 (Nucleoside Diphosphate Sugars); EC 3.6.1.- (Pyrophosphatases); EC 3.6.1.- (nudix hydrolases) |
[Em] Mês de entrada: | 1606 |
[Cu] Atualização por classe: | 170220 |
[Lr] Data última revisão:
| 170220 |
[Sb] Subgrupo de revista: | IM |
[Da] Data de entrada para processamento: | 151103 |
[St] Status: | MEDLINE |
[do] DOI: | 10.1371/journal.pone.0141716 |
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