onr:"swepub:oai:DiVA.org:umu-180769"
Search: onr:"swepub:oai:DiVA.org:umu-180769" > Binding of non-cano...
- 1 of 1
- Previous record
- Next record
- To hitlist
Binding of non-canonical peptidoglycan controls Vibrio cholerae broad spectrum racemase activity
-
- Espaillat, Akbar, master, 1988- (author)
- Umeå universitet,Molekylär Infektionsmedicin, Sverige (MIMS),Umeå Centre for Microbial Research (UCMR),Institutionen för molekylärbiologi (Medicinska fakulteten)
-
- Carrasco-López, Cesar (author)
- Department of Crystallography & Structural Biology, Institute of Physical-Chemistry “Rocasolano”, CSIC, Madrid, Spain
-
- Bernardo-García, Noelia (author)
- Department of Crystallography & Structural Biology, Institute of Physical-Chemistry “Rocasolano”, CSIC, Madrid, Spain
- show more...
- show less...
- (creator_code:org_t)
- Elsevier, 2021
- 2021
- English.
- In: Computational and Structural Biotechnology Journal. - : Elsevier. - 2001-0370. ; 19, s. 1119-1126
- Journal article (peer-reviewed)
Abstract
Subject headings
Close
- Broad-spectrum amino acid racemases (Bsrs) enable bacteria to generate non-canonical D-amino acids (NCDAAs), whose roles and impact on microbial physiology, including modulation of cell wall structure and dissolution of biofilms, are just beginning to be appreciated. Here we used a diverse array of structural, biochemical and molecular simulation studies to define and characterize how BsrV is post-translationally regulated. We discovered that contrary to Vibrio cholerae alanine racemase AlrV highly compacted active site, BsrV’s is broader and can be occupied by cell wall stem peptides. We found that peptidoglycan peptides modified with NCDAAs are better stabilized by BsrV’s catalytic cavity and show better inhibitory capacity than canonical muropeptides. Notably, BsrV binding and inhibition can be recapitulated by undigested peptidoglycan sacculi as it exists in the cell. Docking simulations of BsrV binding the peptidoglycan polymer generate a model where the peptide stems are perfectly accommodated and stabilized within each of the dimeŕs active sites. Taking these biochemical and structural data together, we propose that inhibition of BsrV by peptidoglycan peptides underlies a negative regulatory mechanism to avoid excessive NCDAA production. Our results collectively open the door to use “à la carte” synthetic peptides as a tool to modulate DAAs production of Bsr enzymes.
Subject headings
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinsk bioteknologi -- Medicinsk bioteknologi (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Medical Biotechnology -- Medical Biotechnology (hsv//eng)
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper -- Mikrobiologi inom det medicinska området (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine -- Microbiology in the medical area (hsv//eng)
Keyword
- BsrV
- NCDAA
- Negative feedback loop
- Peptidoglycan
- Vibrio cholera
Publication and Content Type
- ref (subject category)
- art (subject category)
Find in a library
- Computational and Structural Biotechnology Journal (Search for host publication in LIBRIS)
To the university's database
- 1 of 1
- Previous record
- Next record
- To hitlist
Find more in SwePub
- By the author/editor
- Espaillat, Akbar ...
- Carrasco-López, ...
- Bernardo-García, ...
- Rojas-Altuve, Al ...
- Klett, Javier
- Morreale, Antoni ...
- show more...
- Hermoso, Juan A.
- Cava, Felipe
- show less...
- About the subject
-
- MEDICAL AND HEALTH SCIENCES
- MEDICAL AND HEAL ...
- and Medical Biotechn ...
- and Medical Biotechn ...
-
- MEDICAL AND HEALTH SCIENCES
- MEDICAL AND HEAL ...
- and Basic Medicine
- and Microbiology in ...
- Articles in the publication
- Computational an ...
- By the university
- Umeå University
Search outside SwePub
- Extend your search to:
- Google Book Search
- Google Scholar
Kungliga biblioteket hanterar dina personuppgifter i enlighet med EU:s dataskyddsförordning (2018), GDPR. Läs mer om hur det funkar här.
Så här hanterar KB dina uppgifter vid användning av denna tjänst.
- Copyright © LIBRIS - National Library Systems
- LIBRIS.kb.se
