Structural highlights
Function
[RBFA_MYCPN] Associates with free 30S ribosomal subunits (but not with 30S subunits that are part of 70S ribosomes or polysomes). Essential for efficient processing of 16S rRNA. May interact with the 5'-terminal helix region of 16S rRNA (By similarity).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The solution structure of MPN156, a ribosome-binding factor A (RBFA) protein family member from Mycoplasma pneumoniae, is presented. The structure, solved by nuclear magnetic resonance, has a type II KH fold typical of RNA binding proteins. Despite only approximately 20% sequence identity between MPN156 and another family member from Escherichia coli, the two proteins have high structural similarity. The comparison demonstrates that many of the conserved residues correspond to conserved elements in the structures. Compared to a structure based alignment, standard alignment methods based on sequence alone mispair a majority of amino acids in the two proteins. Implications of these discrepancies for sequence based structural modeling are discussed.
Solution structure of a putative ribosome binding protein from Mycoplasma pneumoniae and comparison to a distant homolog.,Rubin SM, Pelton JG, Yokota H, Kim R, Wemmer DE J Struct Funct Genomics. 2003;4(4):235-43. PMID:15185964[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Rubin SM, Pelton JG, Yokota H, Kim R, Wemmer DE. Solution structure of a putative ribosome binding protein from Mycoplasma pneumoniae and comparison to a distant homolog. J Struct Funct Genomics. 2003;4(4):235-43. PMID:15185964
