4X9D
High-resolution structure of Hfq from Methanococcus jannaschii in complex with UMP
Summary for 4X9D
| Entry DOI | 10.2210/pdb4x9d/pdb |
| Related | 4X9C |
| Descriptor | Uncharacterized protein MJ1435, TRIETHYLENE GLYCOL, SULFATE ION, ... (10 entities in total) |
| Functional Keywords | hfq, archaeal lsm, rna binding protein |
| Biological source | Methanocaldococcus jannaschii |
| Total number of polymer chains | 6 |
| Total formula weight | 53038.68 |
| Authors | Nikulin, A.D.,Tishchenko, S.V.,Nikonova, E.Y.,Murina, V.N.,Mihailina, A.O.,Lekontseva, N.V. (deposition date: 2014-12-11, release date: 2015-12-23, Last modification date: 2024-01-10) |
| Primary citation | Nikulin, A.,Mikhailina, A.,Lekontseva, N.,Balobanov, V.,Nikonova, E.,Tishchenko, S. Characterization of RNA-binding properties of the archaeal Hfq-like protein from Methanococcus jannaschii. J. Biomol. Struct. Dyn., 35:1615-1628, 2017 Cited by PubMed Abstract: The Sm and Sm-like proteins are widely distributed among bacteria, archaea and eukarya. They participate in many processes related to RNA-processing and regulation of gene expression. While the function of the bacterial Lsm protein Hfq and eukaryotic Sm/Lsm proteins is rather well studied, the role of Lsm proteins in Archaea is investigated poorly. In this work, the RNA-binding ability of an archaeal Hfq-like protein from Methanococcus jannaschii has been studied by X-ray crystallography, anisotropy fluorescence and surface plasmon resonance. It has been found that MjaHfq preserves the proximal RNA-binding site that usually recognizes uridine-rich sequences. Distal adenine-binding and lateral RNA-binding sites show considerable structural changes as compared to bacterial Hfq. MjaHfq did not bind mononucleotides at these sites and would not recognize single-stranded RNA as its bacterial homologues. Nevertheless, MjaHfq possesses affinity to poly(A) RNA that seems to bind at the unstructured positive-charged N-terminal tail of the protein. PubMed: 27187760DOI: 10.1080/07391102.2016.1189849 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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