DipM controls multiple autolysins and mediates a regulatory feedback loop promoting cell constriction in Caulobacter crescentus

Autor: Adrian Izquierdo-Martinez, Maria Billini, Vega Miguel-Ruano, Rogelio Hernández-Tamayo, Pia Richter, Jacob Biboy, María T. Batuecas, Timo Glatter, Waldemar Vollmer, Peter L. Graumann, Juan A. Hermoso, Martin Thanbichler

Publikováno v: Nature Communications, Vol 14, Iss 1, Pp 1-18 (2023)

Abstract Proteins with a catalytically inactive LytM-type endopeptidase domain are important regulators of cell wall-degrading enzymes in bacteria. Here, we study their representative DipM, a factor promoting cell division in Caulobacter crescentus.

Externí odkaz: https://doaj.org/article/2fa9a82b66fe407c963b0a1c969db130

Catalytic Cycle of Glycoside Hydrolase BglX from Pseudomonas aeruginosa and Its Implications for Biofilm Formation

Autor: Julia Sanz-Aparicio, Mijoon Lee, Kiran V. Mahasenan, María T. Batuecas, Shahriar Mobashery, Choon Kim, Juan A. Hermoso, Jed F. Fisher, Neha Rana, Stefania De Benedetti, Dusan Hesek

Publikováno v: Digital.CSIC. Repositorio Institucional del CSIC
instname

8 pags., 5 figs.
BglX is a heretofore uncharacterized periplasmic glycoside hydrolase (GH) of the human pathogen Pseudomonas aeruginosa. X-ray analysis identifies it as a protein homodimer. The two active sites of the homodimer comprise catalyti

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::23fb3588b071701ca8769f50964297a2
https://doi.org/10.1021/acschembio.9b00754

Crystal Structure and Pathophysiological Role of the Pneumococcal Nucleoside-binding Protein PnrA

Autor: Michael Lalk, Rafael Molina, Franziska Jennert, Stephanie Hirschmann, Sven Hammerschmidt, María T. Batuecas, Philipp Westhoff, Juan A. Hermoso, Franziska Voß, Thomas P. Kohler, Mohammed R. Abdullah

Publikováno v: Digital.CSIC. Repositorio Institucional del CSIC
instname
Digital.CSIC: Repositorio Institucional del CSIC
Consejo Superior de Investigaciones Científicas (CSIC)

19 pags., 7 figs.
Nucleotides are important for RNA and DNA synthesis and, despite a de novo synthesis by bacteria, uptake systems are crucial. Streptococcus pneumoniae, a facultative human pathogen, produces a surface-exposed nucleoside-binding

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bfdd935fc4658fde71110caef738f492
http://hdl.handle.net/10261/240148

Conformational Dynamics in Penicillin-Binding Protein 2a of Methicillin-Resistant Staphylococcus aureus, Allosteric Communication Network and Enablement of Catalysis

Autor: Renee Bouley, María T. Batuecas, Mayland Chang, Jed F. Fisher, Rafael Molina, Shahriar Mobashery, Kiran V. Mahasenan, Juan A. Hermoso

Publikováno v: Digital.CSIC. Repositorio Institucional del CSIC
instname

The mechanism of the β-lactam antibacterials is the functionally irreversible acylation of the enzymes that catalyze the cross-linking steps in the biosynthesis of their peptidoglycan cell wall. The Gram-positive pathogen Staphylococcus aureus uses

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ad315d911cb80d53ececc9cc645283ff
https://doi.org/10.1021/jacs.6b12565

Exolytic and endolytic turnover of peptidoglycan by lytic transglycosylase Slt of

Autor: Mijoon, Lee, María T, Batuecas, Shusuke, Tomoshige, Teresa, Domínguez-Gil, Kiran V, Mahasenan, David A, Dik, Dusan, Hesek, Claudia, Millán, Isabel, Usón, Elena, Lastochkin, Juan A, Hermoso, Shahriar, Mobashery

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America. 115(17)

β-Lactam antibiotics are currently the most broadly used class of antibiotics. These antibiotics prevent bacterial cell wall from cross-linking, which leads to the accumulation of long non–cross-linked strands of peptidoglycan. Pseudomonas aerugin

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::d23f2bc5d315a3186b2f6cf0f0bfae1b
https://pubmed.ncbi.nlm.nih.gov/29632171