Academic Journal

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

التفاصيل البيبلوغرافية
العنوان: Activation by Allostery in Cell-Wall Remodeling by a Modular Membrane-Bound Lytic Transglycosylase from Pseudomonas aeruginosa
المؤلفون: Domínguez-Gil, Teresa, Lee, M., Acebrón, Iván, Mahasenan, Kiran V., Hesek, D., Dik, D.A., Byun, B., Lastochkin, E., Fisher, J.F., Mobashery, S., Hermoso, Juan A.
المساهمون: Ministerio de Economía y Competitividad (España)
سنة النشر: 2016
المجموعة: Digital.CSIC (Consejo Superior de Investigaciones Científicas / Spanish National Research Council)
الوصف: Bacteria 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. ; Peer Reviewed
نوع الوثيقة: article in journal/newspaper
اللغة: unknown
تدمد: 1878-4186
Relation: #PLACEHOLDER_PARENT_METADATA_VALUE#; info:eu-repo/grantAgreement/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/BFU2014/59389-P; Publisher's version; Sí; Structure 24: 1729- 1741 (2016); http://hdl.handle.net/10261/153839; http://dx.doi.org/10.13039/501100003329
DOI: 10.1016/j.str.2016.07.019
DOI: 10.13039/501100003329
الاتاحة: http://hdl.handle.net/10261/153839
https://doi.org/10.1016/j.str.2016.07.019
https://doi.org/10.13039/501100003329
Rights: none
رقم الانضمام: edsbas.9E93F53A
قاعدة البيانات: BASE
الوصف
تدمد:18784186
DOI:10.1016/j.str.2016.07.019