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

Journal Article · Fri Dec 01 04:00:00 EST 2006 · Acta Crystallographica. Section F

DOI:https://doi.org/10.1107/S1744309106044642· OSTI ID:22356429

Caruthers, Jonathan M.; Hu, YaoXiong

The structure of the second helicase domain of the B. subtilis YxiN protein, a DEAD-box RNA helicase, is presented. 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 Å resolution, revealing a parallel αβ-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 recognition of ligands (ATP and RNA) and the coupling of the ATPase activity to conformational changes.

• OSTI ID: 22356429
• Journal Information: Acta Crystallographica. Section F, Journal Name: Acta Crystallographica. Section F Journal Issue: Pt 12 Vol. 62; ISSN ACSFCL; ISSN 1744-3091
• Country of Publication: United Kingdom
• Language: English

Related Subjects

75 CONDENSED MATTER PHYSICS
SUPERCONDUCTIVITY AND SUPERFLUIDITY
AFFINITY
CONFORMATIONAL CHANGES
COUPLING
LIGANDS
RESOLUTION
SPECIFICITY