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1S03

The Structure of a Ribosomal Protein S8/spc Operon mRNA Complex

Summary for 1S03
Entry DOI10.2210/pdb1s03/pdb
Descriptor47-MER, 30S ribosomal protein S8, ZINC ION, ... (4 entities in total)
Functional Keywordsprotein-rna complex, ribosomal, spc operon, transcription-rna complex, transcription/rna
Biological sourceEscherichia coli
More
Total number of polymer chains4
Total formula weight59374.76
Authors
Merianos, H.J.,Wang, J.,Moore, P.B. (deposition date: 2003-12-29, release date: 2004-05-25, Last modification date: 2023-08-23)
Primary citationMerianos, H.J.,Wang, J.,Moore, P.B.
The structure of a ribosomal protein S8/spc operon mRNA complex.
RNA, 10:954-964, 2004
Cited by
PubMed Abstract: In bacteria, translation of all the ribosomal protein cistrons in the spc operon mRNA is repressed by the binding of the product of one of them, S8, to an internal sequence at the 5' end of the L5 cistron. The way in which the first two genes of the spc operon are regulated, retroregulation, is mechanistically distinct from translational repression by S8 of the genes from L5 onward. A 2.8 A resolution crystal structure has been obtained of Escherichia coli S8 bound to this site. Despite sequence differences, the structure of this complex is almost identical to that of the S8/helix 21 complex seen in the small ribosomal subunit, consistent with the hypothesis that autogenous regulation of ribosomal protein synthesis results from conformational similarities between mRNAs and rRNAs. S8 binding must repress the translation of its own mRNA by inhibiting the formation of a ribosomal initiation complex at the start of the L5 cistron.
PubMed: 15146079
DOI: 10.1261/rna.7030704
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.7 Å)
Structure validation

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