3QHS
Crystal structure of full-length Hfq from Escherichia coli
Summary for 3QHS
| Entry DOI | 10.2210/pdb3qhs/pdb |
| Related | 3QO3 |
| Descriptor | Protein hfq (2 entities in total) |
| Functional Keywords | rna binding protein, sm-like, pleiotropic regulator |
| Biological source | Escherichia coli |
| Total number of polymer chains | 12 |
| Total formula weight | 134152.25 |
| Authors | Beich-Frandsen, M.,Vecerek, B.,Sjoeblom, B.,Blaesi, U.,Djinovic-Carugo, K. (deposition date: 2011-01-26, release date: 2011-05-18, Last modification date: 2023-11-01) |
| Primary citation | Beich-Frandsen, M.,Vecerek, B.,Sjoblom, B.,Blasi, U.,Djinovic-Carugo, K. Structural analysis of full-length Hfq from Escherichia coli Acta Crystallogr.,Sect.F, 67:536-540, 2011 Cited by PubMed Abstract: The structure of full-length host factor Qβ (Hfq) from Escherichia coli obtained from a crystal belonging to space group P1, with unit-cell parameters a = 61.91, b = 62.15, c = 81.26 Å, α = 78.6, β = 86.2, γ = 59.9°, was solved by molecular replacement to a resolution of 2.85 Å and refined to R(work) and R(free) values of 20.7% and 25.0%, respectively. Hfq from E. coli has previously been crystallized and the structure has been solved for the N-terminal 72 amino acids, which cover ~65% of the full-length sequence. Here, the purification, crystallization and structural data of the full 102-amino-acid protein are presented. These data revealed that the presence of the C-terminus changes the crystal packing of E. coli Hfq. The crystal structure is discussed in the context of the recently published solution structure of Hfq from E. coli. PubMed: 21543856DOI: 10.1107/S174430911100786X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.85 Å) |
Structure validation
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