The Structures of Mutant Forms of Hfq from Pseudomonas Aeruginosa Reveal the Importance of the Conserved His57 for the Protein Hexamer Organization

Overview

Journal Acta Crystallogr Sect F Struct Biol Cryst Commun

Date 2010 Jul 8

PMID 20606268

Citations 16

Authors

Olga Moskaleva

Bogdan Melnik

Azat Gabdulkhakov

Maria Garber

Stanislav Nikonov

Elena Stolboushkina

Alexei Nikulin

Affiliations

Soon will be listed here.

Abstract

The bacterial Sm-like protein Hfq forms homohexamers both in solution and in crystals. The monomers are organized as a continuous beta-sheet passing through the whole hexamer ring with a common hydrophobic core. Analysis of the Pseudomonas aeruginosa Hfq (PaeHfq) hexamer structure suggested that solvent-inaccessible intermonomer hydrogen bonds created by conserved amino-acid residues should also stabilize the quaternary structure of the protein. In this work, one such conserved residue, His57, in PaeHfq was replaced by alanine, threonine or asparagine. The crystal structures of His57Thr and His57Ala Hfq were determined and the stabilities of all of the mutant forms and of the wild-type protein were measured. The results obtained demonstrate the great importance of solvent-inaccessible conserved hydrogen bonds between the Hfq monomers in stabilization of the hexamer structure.

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