Structure of the second domain of the Bacillus subtilis DEAD-box RNA helicase YxiN.

ABSTRACT: The Bacillus subtilis RNA helicase YxiN is a modular three-domain protein. The first two domains form a conserved helicase core that couples an ATPase activity to an RNA duplex-destabilization activity, while the third domain recognizes a stem-loop of 23S ribosomal RNA with high affinity and specificity. The structure of the second domain, amino-acid residues 207-368, has been solved to 1.95 A resolution, revealing a parallel alphabeta-fold. The crystallographic asymmetric unit contains two protomers; superposition shows that they differ substantially in two segments of peptide that overlap the conserved helicase sequence motifs V and VI, while the remainder of the domain is isostructural. The conformational variability of these segments suggests that induced fit is intrinsic to the recogn

SUBMITTER: Caruthers JM 

PROVIDER: S-EPMC2225381 | biostudies-literature | 2006 Dec

REPOSITORIES: biostudies-literature