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PDBsum entry 2k3f
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Ribosomal protein
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PDB id
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2k3f
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References listed in PDB file
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Key reference
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Title
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Domain reorientation and induced fit upon RNA binding: solution structure and dynamics of ribosomal protein l11 from thermotoga maritima.
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Authors
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S.Ilin,
A.Hoskins,
O.Ohlenschläger,
H.R.Jonker,
H.Schwalbe,
J.Wöhnert.
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Ref.
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Chembiochem, 2005,
6,
1611-1618.
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PubMed id
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Abstract
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L11, a protein of the large ribosomal subunit, binds to a highly conserved
domain of 23S rRNA and mediates ribosomal GTPase activity. Its C-terminal domain
is the main determinant for rRNA binding, whereas its N-terminal domain plays
only a limited role in RNA binding. The N-terminal domain is thought to be
involved in interactions with elongation and release factors as well as with the
antibiotics thiostrepton and micrococcin. This report presents the NMR solution
structure of the full-length L11 protein from the thermophilic eubacterium
Thermotoga maritima in its free form. The structure is based on a large number
of orientational restraints derived from residual dipolar couplings in addition
to conventional NOE-based restraints. The solution structure of L11 demonstrates
that, in contrast to many other multidomain RNA-binding proteins, the relative
orientation of the two domains is well defined. This is shown both by
heteronuclear 15N-relaxation and residual dipolar-coupling data. Comparison of
this NMR structure with the X-ray structure of RNA-bound L11, reveals that
binding not only induces a rigidification of a flexible loop in the C-terminal
domain, but also a sizeable reorientation of the N-terminal domain. The domain
orientation in free L11 shows limited similarity to that of ribosome-bound L11
in complex with elongation factor, EF-G.
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Secondary reference #1
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Title
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L11 domain rearrangement upon binding to RNA and thiostrepton studied by nmr spectroscopy.
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Authors
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H.R.Jonker,
S.Ilin,
S.K.Grimm,
J.Wöhnert,
H.Schwalbe.
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Ref.
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Nucleic Acids Res, 2007,
35,
441-454.
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PubMed id
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