Summary information and primary citation
- PDB-id
-
1cq5;
DSSR-derived features in text and
JSON formats
- Class
- RNA
- Method
- NMR
- Summary
- NMR structure of srp RNA domain iv
- Reference
-
Schmitz U, Behrens S, Freymann DM, Keenan RJ, Lukavsky P,
Walter P, James TL (1999): "Structure
of the phylogenetically most conserved domain of SRP
RNA." RNA, 5, 1419-1429.
doi: 10.1017/S1355838299991458.
- Abstract
- The signal recognition particle (SRP) is a
phylogenetically conserved ribonucleoprotein required for
cotranslational targeting of proteins to the membrane of
the endoplasmic reticulum of the bacterial plasma membrane.
Domain IV of SRP RNA consists of a short stem-loop
structure with two internal loops that contain the most
conserved nucleotides of the molecule. All known essential
interactions of SRP occur in that moiety containing domain
IV. The solution structure of a 43-nt RNA comprising the
complete Escherichia coli domain IV was determined by
multidimensional NMR and restrained molecular dynamics
refinement. Our data confirm the previously determined
rigid structure of a smaller subfragment containing the
most conserved, symmetric internal loop A (Schmitz et al.,
Nat Struct Biol, 1999, 6:634-638), where all conserved
nucleotides are involved in nucleotide-specific structural
interactions. Asymmetric internal loop B provides a hinge
in the RNA molecule; it is partially flexible, yet also
uniquely structured. The longer strand of internal loop B
extends the major groove by creating a ledge-like
arrangement; for loop B however, there is no obvious
structural role for the conserved nucleotides. The
structure of domain IV suggests that loop A is the initial
site for the RNA/protein interaction creating specificity,
whereas loop B provides a secondary interaction site.
