5A5X

Crystal Structure of Se-Met MltF from Pseudomonas aeruginosa

Summary for 5A5X

• Entry DOI: 10.2210/pdb5a5x/pdb
• Descriptor: MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE F, 1,2-ETHANEDIOL, ... (4 entities in total)
• Functional Keywords: hydrolase, lytic transglycosilose, cell wall recycling
• Biological source: PSEUDOMONAS AERUGINOSA PAO1; More
• Cellular location: Cell outer membrane; Peripheral membrane protein: Q9HXN1 Q9HXN1
• Total number of polymer chains: 2
• Total formula weight: 104063.60

Authors

Dominguez-Gil, T.,Acebron, I.,Hermoso, J.A. (deposition date: 2015-06-23, release date: 2016-10-12, Last modification date: 2017-03-22)

Primary citation

Dominguez-Gil, T.,Lee, M.,Acebron-Avalos, I.,Mahasenan, K.V.,Hesek, D.,Dik, D.A.,Byun, B.,Lastochkin, E.,Fisher, J.F.,Mobashery, S.,Hermoso, J.A.
Activation by Allostery in Cell-Wall Remodeling by a Modular Membrane-Bound Lytic Transglycosylase from Pseudomonas aeruginosa.
Structure, 24:1729-1741, 2016

PubMed Abstract: 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.

PubMed: 27618662
DOI: 10.1016/j.str.2016.07.019

Experimental method

X-RAY DIFFRACTION (1.801 Å)