2hjv
From Proteopedia
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Structure of the second domain (residues 207-368) of the Bacillus subtilis YxiN protein
Overview
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.
About this Structure
2HJV is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
Structure of the second domain of the Bacillus subtilis DEAD-box RNA helicase YxiN., Caruthers JM, Hu Y, McKay DB, Acta Crystallograph Sect F Struct Biol Cryst Commun. 2006 Dec 1;62(Pt, 12):1191-5. Epub 2006 Nov 30. PMID:17142894
Page seeded by OCA on Wed Nov 21 11:48:50 2007
