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Structure of HI1333 (YhbY), a Putative RNA-Binding Protein From Haemophilus Influenzae



M A. Willis, W Krajewski, V R. Chalamasetty, Prasad T. Reddy, A J. Howard, O Herzberg


The structures of a number of small [alpha]/[Beta] RNA-binding proteins with diverse biological functions are known1. Their topologies and the locations of the RNA-binding sites vary considerably, consistent with the plasticity of RNA due to base-pair mismatches, bulges and loops. Yet the protein binding surfaces can be recognized because they are enriched with positively charged residues that either form salt bridges with the negatively charged RNA or contribute favorably to the electrostatic environment. Protein regions that exhibit conformational flexibility are also good candidates for RNA-protein interactions since binding is usually accompanied by some mutual conformational adjustments1. We have determined the crystal structure of HI1333 (YhbY) from Haemophilus influenzae, a protein annotated as hypothetical in sequence databases. We propose that this protein and its close sequence relatives (25 in the non-redundant sequence database at the time of writing) comprise a new class of RNA-binding proteins.
Proteins-Structure Function And Genetics
No. 3


function for HI1333, RNA-binding proteins


Willis, M. , Krajewski, W. , Chalamasetty, V. , Reddy, P. , Howard, A. and Herzberg, O. (2002), Structure of HI1333 (YhbY), a Putative RNA-Binding Protein From Haemophilus Influenzae, Proteins-Structure Function And Genetics (Accessed April 22, 2024)
Created October 31, 2002, Updated October 12, 2021