Structure of Pseudomonas aeruginosa Hfq protein

Alexey Nikulin, Elena Stolboushkina, Anna Perederina, Ioulia Vassilieva, Udo Blaesi, Isabella Moll, Galina Kachalova, Shigeyuki Yokoyama, Dmitry Vassylyev, Maria Garber, Stanislav Nikonov

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Abstract

The structure of the Hfq protein from Pseudomonas aeruginosa was determined using two different ionic conditions. In both cases the molecules formed identical hexameric rings, but some variations in the crystal packing were revealed. Hfq belongs to the family of Sm/LSm proteins, the members of which can form hexameric as well as heptameric rings. Comparative analysis of known structures of this protein family shows that the fragment of the Sm-fold responsible for oligomerization is strongly structurally conserved. In the heptameric ring, three conserved hydrogen bonds between β-strands of adjacent molecules hold together the monomers, whereas in the hexameric rings of Hfq an additional conserved inaccessible hydrogen bond between neighbouring monomers is observed.

Original languageEnglish (US)
Pages (from-to)141-146
Number of pages6
JournalActa Crystallographica Section D: Biological Crystallography
Volume61
Issue number2
DOIs
StatePublished - Feb 1 2005

All Science Journal Classification (ASJC) codes

  • Structural Biology

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    Nikulin, A., Stolboushkina, E., Perederina, A., Vassilieva, I., Blaesi, U., Moll, I., Kachalova, G., Yokoyama, S., Vassylyev, D., Garber, M., & Nikonov, S. (2005). Structure of Pseudomonas aeruginosa Hfq protein. Acta Crystallographica Section D: Biological Crystallography, 61(2), 141-146. https://doi.org/10.1107/S0907444904030008