2RLU

The Three Dimensional Structure of the Moorella thermoacetica Selenocysteine Insertion Sequence RNA Hairpin and its Interaction with the Elongation factor SelB

Summary for 2RLU

• Entry DOI: 10.2210/pdb2rlu/pdb
• Related: 1MFK 1WSU
• Descriptor: RNA (5'-R(*GP*GP*UP*UP*GP*CP*GP*GP*GP*UP*CP*UP*CP*GP*CP*AP*AP*CP*C)-3') (1 entity in total)
• Functional Keywords: rna structure, selenocysteine, selb, protein-rna interactions, rna
• Total number of polymer chains: 1
• Total formula weight: 6085.65

Authors

Beribisky, A.V.,Tavares, T.J.,Amborski, A.N.,Motamed, M.,Johnson, A.E.,Mark, T.L.,Johnson, P.E. (deposition date: 2007-08-21, release date: 2008-02-26, Last modification date: 2024-05-01)

Primary citation

Beribisky, A.V.,Tavares, T.J.,Amborski, A.N.,Motamed, M.,Johnson, A.E.,Mark, T.L.,Johnson, P.E.
The three-dimensional structure of the Moorella thermoacetica selenocysteine insertion sequence RNA hairpin and its interaction with the elongation factor SelB
Rna, 13:1948-1956, 2007

PubMed Abstract: Incorporation of the amino acid selenocysteine into a growing protein chain involves the interaction between a hairpin in the mRNA termed the selenocysteine insertion sequence (SECIS) and the special elongation factor SelB. Here we present the structure of the SECIS from the thermophilic organism Moorella thermoacetica (SECIS-MT) determined using nuclear magnetic resonance (NMR) spectroscopy. The SECIS-MT hairpin structure contains a pentaloop with the first and fourth nucleotides of the loop forming a noncanonical GC base pair; the fifth loop nucleotide is bulged out and unstructured. The G and U in positions two and three are on opposite sides of the loop and solvent exposed. The backbone resonances of the SECIS-binding domain from the M. thermoacetica SelB protein were assigned, and the degree of chemical shift perturbations that occur upon SECIS binding were mapped onto the structure of the complex. We demonstrate that a region in the third winged-helix domain of SelB, not previously implicated in binding, is affected by SECIS binding.

PubMed: 17901155
DOI: 10.1261/rna.686607

Experimental method

SOLUTION NMR