1imu
From Proteopedia
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Solution Structure of HI0257, a Ribosome Binding Protein
Overview
A novel bacterial ribosome binding protein, protein Y (also known as, YfiA), was recently shown to reside at the 30S/50S subunit interface and, to stabilize the ribosomal 70S complex against dissociation at low, magnesium ion concentrations. We report here the three-dimensional NMR, structure in solution of a homologue from Haemophilus influenzae, HI0257, that has 64% sequence identity to protein Y. The 107 residue protein has a, beta-alpha-beta-beta-beta-alpha folding topology with two parallel, alpha-helices packed against the same side of a four-stranded beta-sheet., The closest structural relatives are proteins with the double-stranded, RNA-binding domain (dsRBD) motif although there is little (<10%) sequence, homology. The most immediate differences between the dsRBD and HI0257, structures are that (1) HI0257 has a larger beta-sheet motif with an extra, beta-strand at the N-terminus, (2) the helices are parallel in HI0257 but, at an angle of about 30 degrees to each other in the dsRBD, and (3) HI0257, lacks the extended loop commonly seen between the first and second, beta-strands of the dsRBD. Further, an analysis of the surface, electrostatic potential in HI0257 and the dsRBD family reveals significant, differences in the location of contiguous positively (and negatively), charged regions. The structural data, in combination with sequence, analysis of HI0257 and its homologues, suggest that the most likely mode, of RNA recognition for HI0257 may be distinct from that of the dsRBD, family of proteins.
About this Structure
1IMU is a Single protein structure of sequence from Haemophilus influenzae. Full crystallographic information is available from OCA.
Reference
Solution structure of HI0257, a bacterial ribosome binding protein., Parsons L, Eisenstein E, Orban J, Biochemistry. 2001 Sep 18;40(37):10979-86. PMID:11551193
Page seeded by OCA on Tue Nov 20 17:30:35 2007
