4C40

The molecular recognition of kink turn structure by the L7Ae class of proteins

Summary for 4C40

• Entry DOI: 10.2210/pdb4c40/pdb
• Related: 4BW0 4C4W
• Descriptor: 5'-(*GP*GP*CP*GP*AP*AP*GP*AP*AP*CP*CP*GP*GP*GP *GP*AP*GP*CP*C)-3' (2 entities in total)
• Functional Keywords: rna, dna, kink turn
• Biological source: HALOARCULA MARISMORTUI
• Total number of polymer chains: 1
• Total formula weight: 6233.83

Authors

Huang, L.,Lilley, D.M.J. (deposition date: 2013-08-28, 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

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: 24149842
DOI: 10.1261/RNA.041517.113

Experimental method

X-RAY DIFFRACTION (2.2 Å)