Architecture and functional dynamics of the pentafunctional AROM complex

@article{AroraVeraszt2020ArchitectureAF,
  title={Architecture and functional dynamics of the pentafunctional AROM complex},
  author={Harshul Arora Veraszt{\'o} and Maria Logotheti and Reinhard Albrecht and Alexander Leitner and Hongbo Zhu and Marcus D. Hartmann},
  journal={Nature Chemical Biology},
  year={2020},
  pages={1-6}
}
The AROM complex is a multifunctional metabolic machine with ten enzymatic domains catalyzing the five central steps of the shikimate pathway in fungi and protists. We determined its crystal structure and catalytic behavior, and elucidated its conformational space using a combination of experimental and computational approaches. We derived this space in an elementary approach, exploiting an abundance of conformational information from its monofunctional homologs in the Protein Data Bank. It… 
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5 Citations

5 Citations

Microscale Colocalization of Cascade Enzymes Yields Activity Enhancement.
TLDR
This work demonstrates the dependence of the colocalization effect of enzyme cascades on an interplay of nano- and microscales, lending theoretical support to the rational design of highly efficient multienzyme catalysts.
Molecular analysis and essentiality of Aro1 shikimate biosynthesis multi-enzyme in Candida albicans
TLDR
Activity and in cellulo data suggest that only four of Aro1’s enzymatic domains are functional and essential for viability of C. albicans, whereas the 3-dehydroquinate dehydratase (DHQase) domain is inactive because of active site substitutions.
Metabolic channeling: predictions, deductions, and evidence.
Channeling a complex question.
It is generally believed that large protein complexes provide a catalytic advantage due to substrate channeling between enzymatic domains. However, the structure and function of the pentafunctional…
Channeling a complex question
TLDR
The structure and function of the pentafunctional AROM complex suggests a noteworthy exception to the belief that large protein complexes provide a catalytic advantage due to substrate channeling between enzymatic domains.

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