PDBsum entry 2mfl

Ribosomal protein

PDB id: 2mfl

Contents

Protein chain

93 a.a.

PDB id:

2mfl

Name:

Ribosomal protein

Title:

Domain 2 of e. Coli ribosomal protein s1

Structure:

30s ribosomal protein s1. Chain: a. Fragment: unp residues 1-179. Engineered: yes

Source:

Escherichia coli. Organism_taxid: 536056. Strain: k12. Gene: rpsa, ecdh1_2732, ecdh1me8569_0862. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

10 models

Authors:

P.Giraud,J.Crechet,F.Bontems,M.Uzan,C.Sizun

Key ref:

P.Giraud et al. (2015). Resonance assignment of the ribosome binding domain of E. coli ribosomal protein S1. Biomol Nmr Assign, 9, 107-111. PubMed id: 24682851 DOI: 10.1007/s12104-014-9554-2

Date:

12-Oct-13 Release date: 21-May-14

Protein chain

C9QZU1  (C9QZU1_ECOD1) -

DOI no: 10.1007/s12104-014-9554-2

Biomol Nmr Assign 9:107-111 (2015)

PubMed id: 24682851

Resonance assignment of the ribosome binding domain of E. coli ribosomal protein S1.

P.Giraud, J.B.Créchet, M.Uzan, F.Bontems, C.Sizun.

ABSTRACT

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.