4BW0
The molecular recognition of kink turn structure by the L7Ae class of proteins
Summary for 4BW0
Entry DOI | 10.2210/pdb4bw0/pdb |
Related | 4C40 |
Descriptor | HMKT-7, 50S RIBOSOMAL PROTEIN L7AE, SULFATE ION, ... (4 entities in total) |
Functional Keywords | rna-rna binding protein complex, rna/rna binding protein |
Biological source | ARCHAEOGLOBUS FULGIDUS More |
Total number of polymer chains | 2 |
Total formula weight | 22164.87 |
Authors | Huang, L.,Lilley, D.M.J. (deposition date: 2013-06-29, release date: 2013-11-06, Last modification date: 2023-12-20) |
Primary citation | Huang, L.,Lilley, D.M.J. The Molecular Recognition of Kink-Turn Structure by the L7Ae Class of Proteins. RNA, 19:1703-, 2013 Cited by PubMed Abstract: L7Ae is a member of a protein family that binds kink-turns (k-turns) in many functional RNA species. We have solved the X-ray crystal structure of the near-consensus sequence Kt-7 of Haloarcula marismortui bound by Archaeoglobus fulgidus L7Ae at 2.3-Å resolution. We also present a structure of Kt-7 in the absence of bound protein at 2.2-Å resolution. As a result, we can describe a general mode of recognition of k-turn structure by the L7Ae family proteins. The protein makes interactions in the widened major groove on the outer face of the k-turn. Two regions of the protein are involved. One is an α-helix that enters the major groove of the NC helix, making both nonspecific backbone interactions and specific interactions with the guanine nucleobases of the conserved G • A pairs. A hydrophobic loop makes close contact with the L1 and L2 bases, and a glutamate side chain hydrogen bonds with L1. Taken together, these interactions are highly selective for the structure of the k-turn and suggest how conformational selection of the folded k-turn occurs. PubMed: 24149842DOI: 10.1261/RNA.041517.113 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.33 Å) |
Structure validation
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