4mml

D40A Hfq from Pseudomonas aeruginosa

spinqualitylabelsall models 4mml, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4mml is a 1 chain structure with sequence from Pseudomonas aeruginosa PAO1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.801Å Ligands: MG, SO4, U5P Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function HFQ_PSEAE RNA chaperone that binds small regulatory RNA (sRNAs) and mRNAs to facilitate mRNA translational regulation in response to envelope stress, environmental stress and changes in metabolite concentrations. Also binds with high specificity to tRNAs (By similarity). Publication Abstract from PubMed 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. Effect of conserved intersubunit amino Acid substitutions on hfq protein structure and stability.,Murina VN, Melnik BS, Filimonov VV, Uhlein M, Weiss MS, Muller U, Nikulin AD Biochemistry (Mosc). 2014 May;79(5):469-77. doi: 10.1134/S0006297914050113. PMID:24954598 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Protein Hfq 3D structures

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