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Structure paper

TitleStructural basis for the interaction of protein S1 with the Escherichia coli ribosome.
Journal, issue, pagesNucleic Acids Res, Vol. 43, Issue 1, Page 661-673, Year 2015
Publish dateDec 15, 2014
AuthorsKonstantin Byrgazov / Irina Grishkovskaya / Stefan Arenz / Nicolas Coudevylle / Hannes Temmel / Daniel N Wilson / Kristina Djinovic-Carugo / Isabella Moll /
PubMed AbstractIn Gram-negative bacteria, the multi-domain protein S1 is essential for translation initiation, as it recruits the mRNA and facilitates its localization in the decoding centre. In sharp contrast to ...In Gram-negative bacteria, the multi-domain protein S1 is essential for translation initiation, as it recruits the mRNA and facilitates its localization in the decoding centre. In sharp contrast to its functional importance, S1 is still lacking from the high-resolution structures available for Escherichia coli and Thermus thermophilus ribosomes and thus the molecular mechanism governing the S1-ribosome interaction has still remained elusive. Here, we present the structure of the N-terminal S1 domain D1 when bound to the ribosome at atomic resolution by using a combination of NMR, X-ray crystallography and cryo-electron microscopy. Together with biochemical assays, the structure reveals that S1 is anchored to the ribosome primarily via a stabilizing π-stacking interaction within the short but conserved N-terminal segment that is flexibly connected to domain D1. This interaction is further stabilized by salt bridges involving the zinc binding pocket of protein S2. Overall, this work provides one hitherto enigmatic piece in the 'ribosome puzzle', namely the detailed molecular insight into the topology of the S1-ribosome interface. Moreover, our data suggest novel mechanisms that have the potential to modulate protein synthesis in response to environmental cues by changing the affinity of S1 for the ribosome.
External linksNucleic Acids Res / PubMed:25510494 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution2.3 - 9.5 Å
Structure data

EMDB-6211:
Cryo-EM structure of ribosomal protein S1 on the ribosome
Method: EM (single particle) / Resolution: 9.5 Å

PDB-4toi:
Crystal structure of E.coli ribosomal protein S2 in complex with N-terminal domain of S1
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER / Water

Source
  • escherichia coli (E. coli)
  • escherichia coli ta206 (bacteria)
KeywordsRIBOSOMAL PROTEIN / complex / translation

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