Article
The structures of mutant forms of Hfq from Pseudomonas aeruginosa reveal the importance of the conserved His57 for the protein hexamer organization.
Acta crystallographica. Section F, Structural biology and crystallization communications - 1 Jul 2010
Moskaleva Olga, Melnik Bogdan, Gabdulkhakov Azat, Garber Maria, Nikonov Stanislav, Stolboushkina Elena, Nikulin Alexei
Abstract excerpt
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...
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