3M4G

H57A HFQ from Pseudomonas Aeruginosa

Summary for 3M4G

• Entry DOI: 10.2210/pdb3m4g/pdb
• Related: 1U1S 1U1T 3INZ
• Descriptor: Protein hfq, ZINC ION (3 entities in total)
• Functional Keywords: hfq, protein tertiary structure, rna-binding, protein stability, stress response, rna binding protein
• Biological source: Pseudomonas aeruginosa
• Total number of polymer chains: 12
• Total formula weight: 109484.74

Authors

Moskaleva, O.,Melnik, B.,Gabdulkhakov, A.,Garber, M.,Nikonov, S.,Stolboushkina, E.,Nikulin, A. (deposition date: 2010-03-11, release date: 2010-07-28, Last modification date: 2023-09-06)

Primary citation

Moskaleva, O.,Melnik, B.,Gabdulkhakov, A.,Garber, M.,Nikonov, S.,Stolboushkina, E.,Nikulin, A.
The structures of mutant forms of Hfq from Pseudomonas aeruginosa reveal the importance of the conserved His57 for the protein hexamer organization.
Acta Crystallogr.,Sect.F, 66:760-764, 2010

PubMed 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.

PubMed: 20606268
DOI: 10.1107/S1744309110017331

Experimental method

X-RAY DIFFRACTION (2.05 Å)