In:
eLife, eLife Sciences Publications, Ltd, Vol. 7 ( 2018-12-11)
Abstract:
The ubiquitous P-loop fold nucleoside triphosphatases (NTPases) are typically activated by an arginine or lysine ‘finger’. Some of the apparently ancestral NTPases are, instead, activated by potassium ions. To clarify the activation mechanism, we combined comparative structure analysis with molecular dynamics (MD) simulations of Mg-ATP and Mg-GTP complexes in water and in the presence of potassium, sodium, or ammonium ions. In all analyzed structures of diverse P-loop NTPases, the conserved P-loop motif keeps the triphosphate chain of bound NTPs (or their analogs) in an extended, catalytically prone conformation, similar to that imposed on NTPs in water by potassium or ammonium ions. MD simulations of potassium-dependent GTPase MnmE showed that linking of alpha- and gamma phosphates by the activating potassium ion led to the rotation of the gamma-phosphate group yielding an almost eclipsed, catalytically productive conformation of the triphosphate chain, which could represent the basic mechanism of hydrolysis by P-loop NTPases.
Type of Medium:
Online Resource
ISSN:
2050-084X
DOI:
10.7554/eLife.37373.001
DOI:
10.7554/eLife.37373.002
DOI:
10.7554/eLife.37373.003
DOI:
10.7554/eLife.37373.004
DOI:
10.7554/eLife.37373.005
DOI:
10.7554/eLife.37373.006
DOI:
10.7554/eLife.37373.007
DOI:
10.7554/eLife.37373.008
DOI:
10.7554/eLife.37373.009
DOI:
10.7554/eLife.37373.010
DOI:
10.7554/eLife.37373.011
DOI:
10.7554/eLife.37373.012
DOI:
10.7554/eLife.37373.013
DOI:
10.7554/eLife.37373.014
DOI:
10.7554/eLife.37373.015
DOI:
10.7554/eLife.37373.016
DOI:
10.7554/eLife.37373.017
DOI:
10.7554/eLife.37373.018
DOI:
10.7554/eLife.37373.019
DOI:
10.7554/eLife.37373.020
DOI:
10.7554/eLife.37373.021
DOI:
10.7554/eLife.37373.022
DOI:
10.7554/eLife.37373.023
DOI:
10.7554/eLife.37373.024
DOI:
10.7554/eLife.37373.025
DOI:
10.7554/eLife.37373.026
DOI:
10.7554/eLife.37373.027
DOI:
10.7554/eLife.37373.028
DOI:
10.7554/eLife.37373.029
DOI:
10.7554/eLife.37373.033
DOI:
10.7554/eLife.37373.034
Language:
English
Publisher:
eLife Sciences Publications, Ltd
Publication Date:
2018
detail.hit.zdb_id:
2687154-3