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@INPROCEEDINGS{Kelly:1025182,
author = {Kelly, Maria S. and Capelli, Riccardo and Kahawatte,
Shehani and Wijethunga, Hesaree and Carloni, Paolo and Dima,
Ruxandra I.},
title = {{O}ptimizing biophysical predictor selection for katanin
allosteric transitions via metadynamics and machine
learning},
issn = {0006-3495},
reportid = {FZJ-2024-02759},
year = {2024},
abstract = {Katanin, a microtubule-severing enzyme, plays a pivotal
role in regulating cytoskeletal dynamics, cell division, and
intracellular transport. Katanin does this by forming a
hexamer and undergoing a conformational change from its open
“spiral” to closed “ring” state, which enacts
mechanical forces required for the removal of tubulin dimers
from the microtubule lattice. Allosteric regulation has
emerged as a critical aspect of katanin’s functionality,
where binding of ATP and tubulin carboxy-terminal tails
(CTTs) allows katanin to transition from spiral to ring.
Additionally, CTT sequence diversity and post-translational
modifications are known to modulate katanin activity. Thus,
there is a need to learn more about katanin’s allosteric
response to ligand binding to understand its full mechanism.
Here, we ran molecular dynamics simulations of katanin and
surveyed a wide range of biophysical descriptors that reduce
the dimensionality of the all-atomistic output while
allowing us to identify katanin’s allosteric responses to
ligand binding. We studied many physical and chemical
predictors within katanin’s monomeric and hexameric form,
such as solvent accessibility and salt bridge distances,
using machine learning classification algorithms to
attribute large descriptor differences to allosteric
responses from the binding of either ATP or the CTT.
Effective predictors were then utilized as collective
variables for metadynamics simulations, that introduce bias
potentials to aid in the exploration of the free energy
landscape to simulate katanin’s transition from its spiral
to ring configuration. We can then test how the binding of
relevant CTT sequences affects katanin’s free energy
landscape during this transition. In total, we can study the
complexity of allosteric regulation through various
applications using multiple biophysical features of
katanin.},
month = {Feb},
date = {2024-02-10},
organization = {Biophysical Society Meeting,
Philadelphia (USA), 10 Feb 2024 - 14
Feb 2024},
cin = {IAS-5 / INM-9},
ddc = {570},
cid = {I:(DE-Juel1)IAS-5-20120330 / I:(DE-Juel1)INM-9-20140121},
pnm = {5241 - Molecular Information Processing in Cellular Systems
(POF4-524)},
pid = {G:(DE-HGF)POF4-5241},
typ = {PUB:(DE-HGF)1},
doi = {10.1016/j.bpj.2023.11.1698},
url = {https://juser.fz-juelich.de/record/1025182},
}