The structure of Prp2 bound to RNA and ADP-BeF3− reveals structural features important for RNA unwinding by DEAH-box ATPases

Hamann, F.; Zimmerningkat, L.C.; Becker, R.A.; Garbers, T.B.; Neumann, P.; Hub, J.S.; Ficner, R.

doi:10.1107/S2059798321001194

Acta Crystallographica Section D
Acta Crystallographica
Section D STRUCTURAL BIOLOGY

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Figure 3
Comparison of ssRNA binding to spliceosomal DEAH-box ATPases. All ssRNAs bound to spliceosomal DEAH-box ATPases exhibit a kink in the 5′ region. When the RecA2 domains are superimposed [Prp2/Prp43 in (a), Prp2/Prp22 in (b) and Prp43/Prp22 in (c)], the kinks in the Prp43 and Prp22 structures share a similar position and only the kink in the Prp2 structure is differently positioned.

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

Volume 77| Part 4| April 2021| Pages 496-509

https://doi.org/10.1107/S2059798321001194

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