[PMID]: | 23545648 |
[Au] Autor: | Bloudoff K; Schmeing TM |
[Ad] Endereço: | Department of Biochemistry, McGill University, Montréal, QC H3G 0B1, Canada. |
[Ti] Título: | Crystallization and preliminary crystallographic analysis of the first condensation domain of viomycin synthetase. |
[So] Source: | Acta Crystallogr Sect F Struct Biol Cryst Commun;69(Pt 4):412-5, 2013 Apr 01. |
[Is] ISSN: | 1744-3091 |
[Cp] País de publicação: | England |
[La] Idioma: | eng |
[Ab] Resumo: | Nonribosomal peptide synthetases (NRPSs) are large multimodular enzymes that synthesize important secondary metabolites such as antibiotics. NRPSs follow a modular synthetic logic whereby each successive amino-acid monomer is added to the peptide chain by successive multi-domain modules. The condensation domain catalyzes the central chemical event in the synthetic cycle, peptide-bond formation, and is present in every elongation module of the NRPS. Viomycin is an antituberculosis nonribosomal peptide that is synthesized by a series of four NRPS proteins and then modified by tailoring proteins. In order to study the mechanisms of peptide-bond formation in viomycin and in NRPSs in general, a structural study of the first condensation domain of the viomycin synthetase protein VioA (VioA-C1) was initiated. The gene for VioA-C1 was cloned from genomic DNA of Streptomyces vinaceus, expressed as an octahistidine-tagged construct and purified by column chromatography. VioA-C1 was crystallized using the sitting-drop vapor-diffusion method. X-ray diffraction data were collected on a rotating-anode source to 2.9 Å resolution. The data could be indexed in the orthorhombic space group P212121, with unit-cell parameters a = 46.165, b = 68.335, c = 146.423 Å. There is likely to be one monomer in the asymmetric unit, giving a solvent content of 49.2% and a Matthews coefficient (VM) of 2.42 Å(3) Da(-1). Structural determination is in progress. |
[Mh] Termos MeSH primário: |
Peptídeo Sintases/química Streptomyces/enzimologia
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[Mh] Termos MeSH secundário: |
Cristalização Cristalografia por Raios X Peptídeo Sintases/metabolismo Viomicina/biossíntese
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[Pt] Tipo de publicação: | JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T |
[Nm] Nome de substância:
| EC 6.3.2.- (Peptide Synthases); YVU35998K5 (Viomycin) |
[Em] Mês de entrada: | 1312 |
[Cu] Atualização por classe: | 170220 |
[Lr] Data última revisão:
| 170220 |
[Sb] Subgrupo de revista: | IM |
[Da] Data de entrada para processamento: | 130403 |
[St] Status: | MEDLINE |
[do] DOI: | 10.1107/S1744309113004004 |
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