4MMK

Q8A Hfq from Pseudomonas aeruginosa

Summary for 4MMK

• Entry DOI: 10.2210/pdb4mmk/pdb
• Related: 1U1S 3INZ 3M4G 4MML
• Descriptor: Protein hfq, ZINC ION, POTASSIUM ION, ... (6 entities in total)
• Functional Keywords: lsm fold, rna binding protein
• Biological source: Pseudomonas aeruginosa
• Total number of polymer chains: 12
• Total formula weight: 110671.47

Authors

Murina, V.N.,Filimonov, V.V.,Melnik, B.S.,Uhlein, M.,Mueller, U.,Weiss, M.,Nikulin, A.D. (deposition date: 2013-09-09, release date: 2014-07-09, Last modification date: 2023-09-20)

Primary citation

Murina, V.N.,Melnik, B.S.,Filimonov, V.V.,Uhlein, M.,Weiss, M.S.,Muller, U.,Nikulin, A.D.
Effect of conserved intersubunit amino Acid substitutions on hfq protein structure and stability.
Biochemistry Mosc., 79:469-477, 2014

PubMed Abstract: Hfq is a thermostable RNA-binding bacterial protein that forms a uniquely shaped homohexamer. Based on sequence and structural similarity, Hfq belongs to the like-Sm (LSm) protein family. In spite of a rather high degree of homology between archaeal and eukaryotic LSm proteins, their quaternary structure is different, usually consisting of five to eight monomers. In this work, the importance of conserved intersubunit hydrogen bonds for the Hfq spatial organization was tested. The structures and stabilities for the Gln8Ala, Asn28Ala, Asp40Ala, and Tyr55Ala Hfq mutants were determined. All these proteins have the same hexamer organization, but their stability is different. Elimination of a single intersubunit hydrogen bond due to Gln8Ala, Asp40Ala, and Tyr55Ala substitutions results in decreased stability of the Hfq hexamer. Tyr55Ala Hfq as well as the earlier studied His57Ala Hfq has reduced protein thermostability, which seems to correspond to an opening of the protein hydrophobic core.

PubMed: 24954598
DOI: 10.1134/S0006297914050113

Experimental method

X-RAY DIFFRACTION (2.156 Å)