5aa3
From Proteopedia
Crystal structure of MltF from Pseudomonas aeruginosa in the presence of tetrasaccharide and tetrapeptide
Structural highlights
FunctionMLTF_PSEAE Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella.[HAMAP-Rule:MF_02016] Publication Abstract from PubMedBacteria 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 A) 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. Activation by Allostery in Cell-Wall Remodeling by a Modular Membrane-Bound Lytic Transglycosylase from Pseudomonas aeruginosa.,Dominguez-Gil T, Lee M, Acebron-Avalos I, Mahasenan KV, Hesek D, Dik DA, Byun B, Lastochkin E, Fisher JF, Mobashery S, Hermoso JA Structure. 2016 Oct 4;24(10):1729-1741. doi: 10.1016/j.str.2016.07.019. Epub 2016, Sep 8. PMID:27618662[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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