1U1S

Hfq protein from Pseudomonas aeruginosa. Low-salt crystals

Summary for 1U1S

• Entry DOI: 10.2210/pdb1u1s/pdb
• Related: 1HK9 1QK1 1QK2 1U1T
• Descriptor: Hfq protein (2 entities in total)
• Functional Keywords: hfq, hf1, sm-like bacterial protein, riken structural genomics/proteomics initiative, rsgi, structural genomics, rna binding protein
• Biological source: Pseudomonas aeruginosa
• Total number of polymer chains: 6
• Total formula weight: 54686.92

Authors

Nikulin, A.D.,Stolboushkina, E.A.,Perederina, I.,Vassilieva, I.M.,Blaesi, U.,Moll, I.,Kachalova, G.,Vassylyev, D.,Yokoyama, S.,Garber, M.,Nikonov, S.V.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2004-07-16, release date: 2005-01-25, Last modification date: 2023-08-23)

Primary citation

Nikulin, A.,Stolboushkina, E.,Perederina, A.,Vassilieva, I.,Blaesi, U.,Moll, I.,Kachalova, G.,Yokoyama, S.,Vassylyev, D.,Garber, M.,Nikonov, S.
Structure of Pseudomonas aeruginosa Hfq protein.
Acta Crystallogr.,Sect.D, 61:141-146, 2005

PubMed 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 beta-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.

PubMed: 15681864
DOI: 10.1107/S0907444904030008

Experimental method

X-RAY DIFFRACTION (1.6 Å)