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. 1997 Aug 15;16(16):5030–5036. doi: 10.1093/emboj/16.16.5030

Crystal structure of a new RNA-binding domain from the antiterminator protein SacY of Bacillus subtilis.

H van Tilbeurgh 1, X Manival 1, S Aymerich 1, J M Lhoste 1, C Dumas 1, M Kochoyan 1
PMCID: PMC1170137  PMID: 9305644

Abstract

SacY belongs to a family of, at present, seven bacterial transcriptional antiterminators. The RNA-binding and antitermination capacity of SacY resides in the 55 amino acids at the N-terminal [SacY(1-55)]. The crystal structure at 2 A resolution shows that SacY(1-55) forms a dimer in the crystal, in accordance with the NMR solution structure. The structure of the monomer is a four-stranded beta-sheet with a simple beta1beta2beta3beta4 topology. One side of the sheet is covered by a long surface loop and the other side forms the dimer interface. The dimer is stabilized by the orthogonal stacking of the two beta-sheets. The crystal structure is in excellent agreement with the NMR solution structure (r.m.s. distance for C alpha coordinates is 1.3 A). The structure of SacY(1-55) reveals a new RNA-binding motif.

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Selected References

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