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The crystal structure of Mycobacterium thermoresistibile MurE ligase reveals the binding mode of the substrate m-diaminopimelate.
Rossini, Nicolas de Oliveira; Silva, Catharina; Dias, Marcio Vinicius Bertacine.
Afiliação
  • Rossini NO; Department of Microbiology, Institute of Biomedical Science, University of São Paulo, Av. Prof Lineu Prestes, 1374, CEP 05508-000 São Paulo, SP, Brazil.
  • Silva C; Department of Microbiology, Institute of Biomedical Science, University of São Paulo, Av. Prof Lineu Prestes, 1374, CEP 05508-000 São Paulo, SP, Brazil.
  • Dias MVB; Department of Microbiology, Institute of Biomedical Science, University of São Paulo, Av. Prof Lineu Prestes, 1374, CEP 05508-000 São Paulo, SP, Brazil; Department of Chemistry. The University of Warwick, Coventry CV4 7AL, UK. Electronic address: mvbdias@usp.br.
J Struct Biol ; 215(2): 107957, 2023 06.
Article em En | MEDLINE | ID: mdl-36944394
The cytoplasmatic biosynthesis of the stem peptide from the peptidoglycan in bacteria involves six steps, which have the role of three ATP-dependent Mur ligases that incorporate three consecutive amino acids to a substrate precursor. MurE is the last Mur ligase to incorporate a free amino acid. Although the structure of MurE from Mycobacterium tuberculosis (MtbMurE) was determined at 3.0 Å, the binding mode of meso-Diaminopimelate (m-DAP) and the effect of substrate absence is unknown. Herein, we show the structure of MurE from M. thermoresistibile (MthMurE) in complex with ADP and m-DAP at 1.4 Å resolution. The analysis of the structure indicates key conformational changes that the substrate UDP-MurNAc-L-Ala-D-Glu (UAG) and the free amino acid m-DAP cause on the MthMurE conformation. We observed several movements of domains or loop regions that displace their position in order to perform enzymatic catalysis. Since MthMurE has a high similarity to MtbMurE, this enzyme could also guide strategies for structure-based antimicrobial discovery to fight against tuberculosis or other mycobacterial infections.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Peptídeo Sintases / Mycobacterium tuberculosis Idioma: En Revista: J Struct Biol Assunto da revista: BIOLOGIA MOLECULAR Ano de publicação: 2023 Tipo de documento: Article País de afiliação: Brasil País de publicação: Estados Unidos
Texto completo
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XML
PubMed Links
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Peptídeo Sintases / Mycobacterium tuberculosis Idioma: En Revista: J Struct Biol Assunto da revista: BIOLOGIA MOLECULAR Ano de publicação: 2023 Tipo de documento: Article País de afiliação: Brasil País de publicação: Estados Unidos