Membrane enzymes: transformers at the interface.

@article{Brodhun2015MembraneET,
  title={Membrane enzymes: transformers at the interface.},
  author={Florian Brodhun and Kai Tittmann},
  journal={Nature chemical biology},
  year={2015},
  volume={11 2},
  pages={
          102-3
        }
}
Recent studies on two enzyme classes operating at the membrane interface showcase an unanticipated degree of structural plasticity involving domain swapping and marked secondary structure reshuffling. This structural variability in topology is key to functional diversification and catalytic prowess. 
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Dissecting the Structural and Chemical Determinants of the "Open-to-Closed" Motion in the Mannosyltransferase PimA from Mycobacteria.
TLDR
A series of chemical derivatives were analyzed to determine the structural contribution of the mannose ring in such an activation mechanism and contribute to a better understanding of the structural determinants involved in the "open-to-closed" motion not only observed in PimA but also visualized and/or predicted in other glycosyltransfeases.
Molecular Basis of Membrane Association by the Phosphatidylinositol Mannosyltransferase PimA Enzyme from Mycobacteria*
TLDR
This work determined that PimA preferentially binds to negatively charged phosphatidyl-myo-inositol substrate and non-substrate membrane model systems through its N-terminal domain, inducing an important structural reorganization of anionic phospholipids.
Structural basis of phosphatidyl-myo-inositol mannosides biosynthesis in mycobacteria.

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Competing financial interests The authors declare no competing financial interests. np g © 2 01 5 N at ur e A m er ic a, In c. A ll rig
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