1d6k
From Proteopedia
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NMR SOLUTION STRUCTURE OF THE 5S RRNA E-LOOP/L25 COMPLEX
Overview
The structure of the complex between ribosomal protein L25 and a 37, nucleotide RNA molecule, which contains the E-loop and helix IV regions of, the E-domain of Escherichia coli 5S rRNA, has been determined to an, overall r.m.s. displacement of 1.08 A (backbone heavy atoms) by, heteronuclear NMR spectroscopy (Protein Databank code 1d6k). The, interacting molecular surfaces are bipartite for both the RNA and the, protein. One side of the six-stranded beta-barrel of L25 recognizes the, minor groove of the E-loop with very little change in the conformations of, either the protein or the RNA and with the RNA-protein interactions, occurring mainly along one strand of the E-loop duplex. This minor groove, recognition module includes two parallel beta-strands of L25, a hitherto, unknown RNA binding topology. Binding of the RNA also induces conversion, of a flexible loop to an alpha-helix in L25, the N-terminal tip of which, interacts with the widened major groove at the E-loop/helix IV junction of, the RNA. The structure of the complex reveals that the E-domain RNA serves, as a preformed docking partner, while the L25 protein has one preformed, and one induced recognition module.
About this Structure
1D6K is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
The NMR structure of the 5S rRNA E-domain-protein L25 complex shows preformed and induced recognition., Stoldt M, Wohnert J, Ohlenschlager O, Gorlach M, Brown LR, EMBO J. 1999 Nov 15;18(22):6508-21. PMID:10562563
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