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PDBsum entry 2mfl
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Ribosomal protein
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PDB id
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2mfl
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References listed in PDB file
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Key reference
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Title
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Resonance assignment of the ribosome binding domain of e. Coli ribosomal protein s1.
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Authors
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P.Giraud,
J.B.Créchet,
M.Uzan,
F.Bontems,
C.Sizun.
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Ref.
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Biomol Nmr Assign, 2015,
9,
107-111.
[DOI no: ]
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PubMed id
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Abstract
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Ribosomal protein S1 is an essential actor for protein synthesis in Escherichia
coli. It is involved in mRNA recruitment by the 30S ribosomal subunit and
recognition of the correct start codon during translation initiation. E. coli S1
is a modular protein that contains six repeats of an S1 motif, which have
distinct functions despite structural homology. Whereas the three central
repeats have been shown to be involved in mRNA recognition, the two first
repeats that constitute the N-terminal domain of S1 are responsible for binding
to the 30S subunit. Here we report the almost complete (1)H, (13)C and (15)N
resonance assignment of two fragments of the 30S binding region of S1. The first
fragment comprises only the first repeat. The second corresponds to the entire
ribosome binding domain. Since S1 is absent from all high resolution X-ray
structures of prokaryotic ribosomes, these data provide a first step towards
atomic level structural characterization of this domain by NMR. Chemical shift
analysis of the first repeat provides evidence for structural divergence from
the canonical OB-fold of an S1 motif. In contrast the second domain displays the
expected topology for an S1 motif, which rationalizes the functional
specialization of the two subdomains.
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