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  • Espaillat, Akbar,master,1988-Umeå universitet,Molekylär Infektionsmedicin, Sverige (MIMS),Umeå Centre for Microbial Research (UCMR),Institutionen för molekylärbiologi (Medicinska fakulteten),Chr. Hansen A/S, Microbial Physiology, R & amp;D, Hoersholm, Denmark (author)

A distinctive family of L,D-transpeptidases catalyzing L-Ala-mDAP crosslinks in Alpha- and Betaproteobacteria

  • Article/chapterEnglish2024

Publisher, publication year, extent ...

  • Springer Nature,2024
  • electronicrdacarrier

Numbers

  • LIBRIS-ID:oai:DiVA.org:umu-221654
  • https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-221654URI
  • https://doi.org/10.1038/s41467-024-45620-5DOI

Supplementary language notes

  • Language:English
  • Summary in:English

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  • Subject category:ref swepub-contenttype
  • Subject category:art swepub-publicationtype

Notes

  • The bacterial cell-wall peptidoglycan is made of glycan strands crosslinked by short peptide stems. Crosslinks are catalyzed by DD-transpeptidases (4,3-crosslinks) and LD-transpeptidases (3,3-crosslinks). However, recent research on non-model species has revealed novel crosslink types, suggesting the existence of uncharacterized enzymes. Here, we identify an LD-transpeptidase, LDTGo, that generates 1,3-crosslinks in the acetic-acid bacterium Gluconobacter oxydans. LDTGo-like proteins are found in Alpha- and Betaproteobacteria lacking LD3,3-transpeptidases. In contrast with the strict specificity of typical LD- and DD-transpeptidases, LDTGo can use non-terminal amino acid moieties for crosslinking. A high-resolution crystal structure of LDTGo reveals unique features when compared to LD3,3-transpeptidases, including a proline-rich region that appears to limit substrate access, and a cavity accommodating both glycan chain and peptide stem from donor muropeptides. Finally, we show that DD-crosslink turnover is involved in supplying the necessary substrate for LD1,3-transpeptidation. This phenomenon underscores the interplay between distinct crosslinking mechanisms in maintaining cell wall integrity in G. oxydans.

Subject headings and genre

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  • Alvarez, LauraUmeå universitet,Molekylär Infektionsmedicin, Sverige (MIMS),Umeå Centre for Microbial Research (UCMR),Institutionen för molekylärbiologi (Medicinska fakulteten)(Swepub:umu)laal0007 (author)
  • Torrens, GabrielUmeå universitet,Molekylär Infektionsmedicin, Sverige (MIMS),Umeå Centre for Microbial Research (UCMR),Institutionen för molekylärbiologi (Medicinska fakulteten)(Swepub:umu)gato0010 (author)
  • ter Beek, JosyUmeå universitet,Institutionen för medicinsk kemi och biofysik,Wallenberg centrum för molekylär medicin vid Umeå universitet (WCMM)(Swepub:umu)jote0033 (author)
  • Miguel-Ruano, VegaDepartment of Crystallography and Structural Biology, Institute of Physical Chemistry “Blas Cabrera”, CSIC, Madrid, Spain (author)
  • Irazoki, OihaneUmeå universitet,Molekylär Infektionsmedicin, Sverige (MIMS),Umeå Centre for Microbial Research (UCMR),Institutionen för molekylärbiologi (Medicinska fakulteten)(Swepub:umu)oiir0001 (author)
  • Gago, FedericoDepartment of Biomedical Sciences & amp; IQM-CSIC Associate Unit, School of Medicine and Health Sciences, University of Alcalá, Alcalá de Henares, Madrid, Spain (author)
  • Hermoso, Juan A.Department of Crystallography and Structural Biology, Institute of Physical Chemistry “Blas Cabrera”, CSIC, Madrid, Spain (author)
  • Berntsson, Ronnie P-A.Umeå universitet,Institutionen för medicinsk kemi och biofysik,Wallenberg centrum för molekylär medicin vid Umeå universitet (WCMM)(Swepub:umu)robe0049 (author)
  • Cava, FelipeUmeå universitet,Molekylär Infektionsmedicin, Sverige (MIMS),Umeå Centre for Microbial Research (UCMR),Institutionen för molekylärbiologi (Medicinska fakulteten)(Swepub:umu)feca0003 (author)
  • Umeå universitetMolekylär Infektionsmedicin, Sverige (MIMS) (creator_code:org_t)

Related titles

  • In:Nature Communications: Springer Nature15:12041-1723

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