1nmu
From Proteopedia
MBP-L30
Overview
The Saccharomyces cerevisiae ribosomal protein L30 autoregulates its own expression by binding to a purine-rich internal loop in its pre-mRNA and mRNA. NMR studies of L30 and its RNA complex showed that both the internal loop of the RNA as well as a region of the protein become substantially more ordered upon binding. A crystal structure of a maltose binding protein (MBP)-L30 fusion protein with two copies in the asymmetric unit has been determined. The flexible RNA-binding region in the L30 copies has two distinct conformations, one resembles the RNA bound form solved by NMR and the other is unique. Structure prediction algorithms also had difficulty accurately predicting this region, which is consistent with conformational flexibility seen in the NMR and X-ray crystallography studies. Inherent conformational flexibility may be a hallmark of regions involved in intermolecular interactions.
About this Structure
1NMU is a Protein complex structure of sequences from Escherichia coli and Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Inherent protein structural flexibility at the RNA-binding interface of L30e., Chao JA, Prasad GS, White SA, Stout CD, Williamson JR, J Mol Biol. 2003 Feb 28;326(4):999-1004. PMID:12589748 Page seeded by OCA on Sat May 3 02:43:25 2008
