Crystal structures of the archaeal RNase P protein Rpp38 in complex with RNA fragments containing a K-turn motif

Oshima, K.; Gao, X.; Hayashi, S.; Ueda, T.; Nakashima, T.; Kimura, M.

doi:10.1107/S2053230X17018039

Acta Crystallographica Section F
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

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Figure 3
Interfaces for protein–RNA interactions. The hydrogen-bonding network for PhoRpp38 bound to the P12.2M K-turn. (a) Lys35 in β1 and Thr37, Asn38, Glu39 and Lys42 in α2 form a hydrogen-bond network with nucleotide residues in the NC helix. (b) Glu94, Ala96 and Ala98 in the loop between α4 and β4 bind G17 and G18 in the 3 nt bulge, and Asp59 and Lys84 hydrogen-bond U19 in the 3 nt bulge. PhoRpp38 and P12.2M are presented in cartoon representation, while the amino-acid residues involved in the interaction are shown in stick representation.

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 74| Part 1| January 2018| Pages 57-64

https://doi.org/10.1107/S2053230X17018039

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