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PDBsum entry 1cql
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References listed in PDB file
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Key reference
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Title
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Structure of the phylogenetically most conserved domain of srp RNA.
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Authors
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U.Schmitz,
S.Behrens,
D.M.Freymann,
R.J.Keenan,
P.Lukavsky,
P.Walter,
T.L.James.
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Ref.
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Rna, 1999,
5,
1419-1429.
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PubMed id
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Abstract
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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.
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Headers
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