English   español  
Por favor, use este identificador para citar o enlazar a este item: http://hdl.handle.net/10261/153839
COMPARTIR / IMPACTO:
Estadísticas
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar a otros formatos:
Título

Activation by Allostery in Cell-Wall Remodeling by a Modular Membrane-Bound Lytic Transglycosylase from Pseudomonas aeruginosa

AutorDomínguez-Gil, Teresa; Lee, M.; Acebrón, Iván ; Mahasenan, K.V.; Hesek, D.; Dik, D.A.; Byun, B.; Lastochkin, E.; Fisher, J.F.; Mobashery, S.; Hermoso, Juan A.
Fecha de publicación2016
CitaciónStructure 24: 1729- 1741 (2016)
ResumenBacteria grow and divide without loss of cellular integrity. This accomplishment is notable, as a key component of their cell envelope is a surrounding glycopeptide polymer. In Gram-negative bacteria this polymer—the peptidoglycan—grows by the difference between concurrent synthesis and degradation. The regulation of the enzymatic ensemble for these activities is poorly understood. We report herein the structural basis for the control of one such enzyme, the lytic transglycosylase MltF of Pseudomonas aeruginosa. Its structure comprises two modules: an ABC-transporter-like regulatory module and a catalytic module. Occupancy of the regulatory module by peptidoglycan-derived muropeptides effects a dramatic and long-distance (40 Å) conformational change, occurring over the entire protein structure, to open its active site for catalysis. This discovery of the molecular basis for the allosteric control of MltF catalysis is foundational to further study of MltF within the complex enzymatic orchestration of the dynamic peptidoglycan.
URIhttp://hdl.handle.net/10261/153839
DOI10.1016/j.str.2016.07.019
Identificadoresdoi: 10.1016/j.str.2016.07.019
issn: 1878-4186
Aparece en las colecciones: (IQFR) Artículos
Ficheros en este ítem:
Fichero Descripción Tamaño Formato  
accesoRestringido.pdf15,38 kBAdobe PDFVista previa
Visualizar/Abrir
Mostrar el registro completo
 

Artículos relacionados:


NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.