{"ok":true,"nota":{"id":"678c6d3e6332e60f","slug":"logran-fotografiar-en-detalle-la-maquina-bacteriana-que-arma-las-prote-678c6d","titulo":"Logran fotografiar en detalle la máquina bacteriana que arma las proteínas de su membrana","resumen":"Científicos usaron microscopía crioelectrónica para captar la forma tridimensional de la BAM, el complejo que ensambla proteínas en la membrana externa de las bacterias gramnegativas. Obtuvieron imágenes en distintos detergentes y en nanodiscos con lípidos bacterianos, lo que permitió ver cómo cierra su compuerta lateral.","fuente":"biorxiv","fuenteNombre":"bioRxiv · preprints","color":"#be2628","autor":"Kato, T., Shigematsu, H., Takeuchi, K., Suzuki, M., Nitta, R., Imasaki, T.","url":"https://www.biorxiv.org/content/10.64898/2026.10.20.760484v1?rss=1","imagen":"/hoy/portada/678c6d3e6332e60f","tema":"ciencia","subtemas":["bacterias","membrana externa","microscopía crioelectrónica","resistencia a antibióticos","biología estructural"],"entidades":["bioRxiv","Escherichia coli"],"formato":"dato","entretenimiento":false,"pubTs":"2026-10-21T00:00:00.000Z","indexTs":"2026-10-21T22:39:37.287Z","hash":"fdeded44ace7e6a0c79fccd65627e1dbb21a198e5b17fc6377861d5de81cc706","tsa":{"time":"Oct 21 22:40:36 2026 GMT","provider":"freetsa.org","sobre":"sello"},"stats":{"views":0,"likes":0,"clicks":0,"dwell":0},"tipo":"normal","registro":"hallazgo","porQueImporta":"Las bacterias gramnegativas son las responsables de muchas infecciones difíciles de tratar, en parte porque su membrana externa las protege de los antibióticos. Conocer cómo se arma esa membrana ayuda a pensar nuevos fármacos que la bloqueen. Para un lector de acá, el dato concreto es que se logró ver la máquina en un entorno más parecido al natural, y eso reduce el margen de error en el diseño de futuras drogas. Aun así, es un avance de base: transformarlo en un antibiótico concreto demanda años de investigación.","quienFirma":"bioRxiv · preprints","confianza":"preprint","consulta":null},"sello":{"hash":"fdeded44ace7e6a0c79fccd65627e1dbb21a198e5b17fc6377861d5de81cc706","sello":"e348a9c5270d25ceb0d2d47cdd8c359875c7c7c86bfb6f7ad34da0c1c0907c6e","beacon":{"drand":{"cadena":"8990e7a9aaed2ffed73dbd7092123d6f289930540d7651336225dc172e51b2ce","ronda":6573046,"aleatorio":"f71b3db032f12c8ae2d90f38aa37ddc03a4bd072f8a3317f2962e831c62e695d","tiempo":"2026-10-21T22:40:00.000Z"},"nist":{"cadena":2,"pulso":1993728,"salida":"DBB029F00A75EEAA9AF69BB0B3207AD12D5A4EDD2136CB35D25CB332980962472F1AFBB0B247EB7DF6BE52045BC8A63F1D14E2719075ECD2BA39DE673005A0E1","tiempo":"2026-10-21T22:39:00.000Z"},"noAntes":"2026-10-21T22:40:00.000Z"},"verificacion":{"drand":true,"nist":true},"tsa":{"time":"Oct 21 22:40:36 2026 GMT","provider":"freetsa.org","sobre":"sello"},"original":{"titulo":"CLOSING THE CONFORMATIONAL CYCLE OF THE BETA-BARREL ASSEMBLY MACHINERY","descripcion":"The {beta}-barrel assembly machinery (BAM) catalyzes the folding and insertion of {beta}-barrel outer membrane proteins (OMPs) in Gram-negative bacteria without an external energy source. BAM comprises the central subunit BamA and associated lipoproteins, with BamA forming a conformationally dynamic lateral gate. Although substrate-engaged structures have revealed key steps in OMP assembly, how substrate-free BamA closes its lateral gate and which conformations it adopts in a lipid bilayer remain unclear. Here, we determined cryo-EM structures of the Escherichia coli (E. coli) BAM complex in three detergents and in Saposin A nanodiscs composed of E. coli polar lipids. In addition to the cano","pubDate":"2026-10-21","url":"https://www.biorxiv.org/content/10.64898/2026.10.20.760484v1?rss=1"},"indexado":"2026-10-21T22:39:37.287Z"}}