2HJV

Structure of the second domain (residues 207-368) of the Bacillus subtilis YxiN protein

Summary for 2HJV

• Entry DOI: 10.2210/pdb2hjv/pdb
• Related: 2G0C
• Descriptor: ATP-dependent RNA helicase dbpA (2 entities in total)
• Functional Keywords: parallel alpha-beta, hydrolase
• Biological source: Bacillus subtilis
• Cellular location: Cytoplasm (Probable): P42305
• Total number of polymer chains: 2
• Total formula weight: 37352.35

Authors

McKay, D.B.,Caruthers, J.M. (deposition date: 2006-07-02, release date: 2006-12-12, Last modification date: 2023-08-30)

Primary citation

Caruthers, J.M.,Hu, Y.,McKay, D.B.
Structure of the second domain of the Bacillus subtilis DEAD-box RNA helicase YxiN.
Acta Crystallogr.,Sect.F, 62:1191-1195, 2006

PubMed 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 recognition of ligands (ATP and RNA) and the coupling of the ATPase activity to conformational changes.

PubMed: 17142894
DOI: 10.1107/S1744309106044642

Experimental method

X-RAY DIFFRACTION (1.95 Å)