Long-residency hydration, cation binding, and dynamics of loop E/helix IV rRNA-L25 protein complex.

Abstract:

:Molecular dynamics simulations of RNA-protein complex between Escherichia coli loop E/helix IV (LE/HeIV) rRNA and L25 protein reveal a qualitative agreement between the experimental and simulated structures. The major groove of LE is a prominent rRNA cation-binding site. Divalent cations rigidify the LE major groove geometry whereas in the absence of divalent cations LE extensively interacts with monovalent cations via inner-shell binding. The HeIV region shows bistability of its major groove explaining the observed differences between x-ray and NMR structures. In agreement with the experiments, the simulations suggest that helix-alpha1 of L25 is the least stable part of the protein. Inclusion of Mg2+ cations into the simulations causes perturbation of basepairing at the LE/HeIV junction, which does not, however, affect the protein binding. The rRNA-protein complex is mediated by a number of highly specific hydration sites with long-residing water molecules and two of them are bound throughout the entire 24-ns simulation. Long-residing water molecules are seen also outside the RNA-protein contact areas with water-binding times substantially enhanced compared to simulations of free RNA. Long-residency hydration sites thus represent important elements of the three-dimensional structure of rRNA.

journal_name

Biophys J

journal_title

Biophysical journal

authors

Réblová K,Spacková N,Koca J,Leontis NB,Sponer J

doi

10.1529/biophysj.104.047126

subject

Has Abstract

pub_date

2004-11-01 00:00:00

pages

3397-412

issue

5

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(04)73805-9

journal_volume

87

pub_type

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