J
Juan A. Hermoso
Researcher at Spanish National Research Council
Publications - 200
Citations - 6692
Juan A. Hermoso is an academic researcher from Spanish National Research Council. The author has contributed to research in topics: Peptidoglycan & Lipase. The author has an hindex of 42, co-authored 189 publications receiving 5948 citations. Previous affiliations of Juan A. Hermoso include Centre national de la recherche scientifique & University of Arizona.
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Taking aim on bacterial pathogens: from phage therapy to enzybiotics
TL;DR: Endolysins are considered as effective antimicrobials with potentially important applications in medicine and biotechnology because of the surprising rich structural catalytic diversity of these murein hydrolases.
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Crystal and Electron Microscopy Structures of Sticholysin II Actinoporin Reveal Insights into the Mechanism of Membrane Pore Formation
José M. Mancheño,Jaime Martín-Benito,Martín Martínez-Ripoll,José G. Gavilanes,Juan A. Hermoso +4 more
TL;DR: It is found that StnII exists in a monomeric soluble state but forms tetramers in the presence of a lipidic interface, and the structural basis for the membrane recognition step of actinoporins and unexpected insights into the oligomerization step are provided.
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How allosteric control of Staphylococcus aureus penicillin binding protein 2a enables methicillin resistance and physiological function
Lisandro H. Otero,Alzoray Rojas-Altuve,Leticia I. Llarrull,César Carrasco-López,Malika Kumarasiri,Elena Lastochkin,Jennifer Fishovitz,Matthew Dawley,Dusan Hesek,Mijoon Lee,Jarrod W. Johnson,Jed F. Fisher,Mayland Chang,Shahriar Mobashery,Juan A. Hermoso +14 more
TL;DR: The identification of an allosteric binding domain—a remarkable 60 Å distant from the dd-transpeptidase active site—discovered by crystallographic analysis of a soluble construct of PBP2a opens an unprecedented realm for β-lactam antibiotic structure-based design.
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Lipase activation by nonionic detergents. The crystal structure of the porcine lipase-colipase-tetraethylene glycol monooctyl ether complex.
Juan A. Hermoso,David Pignol,Brigitte Kerfelec,Isabelle Crenon,Catherine Chapus,Juan C. Fontecilla-Camps +5 more
TL;DR: The crystal structure of the ternary porcine lipase-colipase-tetra ethylene glycol monooctyl ether complex has been determined and it is shown that TGME acts as a substrate analog, thus possibly explaining the inhibitory effect of this nonionic detergent on emulsified substrate hydrolysis at submicellar concentrations.
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Activation of Bacterial Thermoalkalophilic Lipases Is Spurred by Dramatic Structural Rearrangements
César Carrasco-López,César A. Godoy,Blanca de las Rivas,Gloria Fernández-Lorente,Jose M. Palomo,Jose M. Guisan,Roberto Fernandez-Lafuente,Martín Martínez-Ripoll,Juan A. Hermoso +8 more
TL;DR: The combination of structural and biochemical studies indicate that the lid opening is not mediated by temperature but triggered by interaction with lipid substrate, and the first structure of a member of the lipase family I.5 showing an open configuration is reported.