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A distinctive famil...
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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 ...
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Springer Nature,2024
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electronicrdacarrier
Numbers
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LIBRIS-ID:oai:DiVA.org:umu-221654
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https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-221654URI
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https://doi.org/10.1038/s41467-024-45620-5DOI
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Language:English
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Summary in:English
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Subject category:ref swepub-contenttype
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Subject category:art swepub-publicationtype
Notes
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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.
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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)
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Torrens, GabrielUmeå universitet,Molekylär Infektionsmedicin, Sverige (MIMS),Umeå Centre for Microbial Research (UCMR),Institutionen för molekylärbiologi (Medicinska fakulteten)(Swepub:umu)gato0010
(author)
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ter Beek, JosyUmeå universitet,Institutionen för medicinsk kemi och biofysik,Wallenberg centrum för molekylär medicin vid Umeå universitet (WCMM)(Swepub:umu)jote0033
(author)
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Miguel-Ruano, VegaDepartment of Crystallography and Structural Biology, Institute of Physical Chemistry “Blas Cabrera”, CSIC, Madrid, Spain
(author)
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Irazoki, OihaneUmeå universitet,Molekylär Infektionsmedicin, Sverige (MIMS),Umeå Centre for Microbial Research (UCMR),Institutionen för molekylärbiologi (Medicinska fakulteten)(Swepub:umu)oiir0001
(author)
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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)
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Hermoso, Juan A.Department of Crystallography and Structural Biology, Institute of Physical Chemistry “Blas Cabrera”, CSIC, Madrid, Spain
(author)
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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)
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Cava, FelipeUmeå universitet,Molekylär Infektionsmedicin, Sverige (MIMS),Umeå Centre for Microbial Research (UCMR),Institutionen för molekylärbiologi (Medicinska fakulteten)(Swepub:umu)feca0003
(author)
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Umeå universitetMolekylär Infektionsmedicin, Sverige (MIMS)
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In:Nature Communications: Springer Nature15:12041-1723
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Espaillat, Akbar ...
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Alvarez, Laura
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Torrens, Gabriel
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ter Beek, Josy
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Miguel-Ruano, Ve ...
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Irazoki, Oihane
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Gago, Federico
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Hermoso, Juan A.
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