DSSR-PyMOL cartoon-block schematics: PDB entry 4tuw

PDB-id

4tuw; DSSR-derived features in text and JSON formats

Class

RNA binding protein-RNA

Method

X-ray (2.902 Å)

Summary

Drosophila stem-loop binding protein complexed with histone mrna stem-loop, phospho mimic of tpnk and c-terminal region

Reference

Zhang J, Tan D, DeRose EF, Perera L, Dominski Z, Marzluff WF, Tong L, Hall TM (2014): "Molecular mechanisms for the regulation of histone mRNA stem-loop-binding protein by phosphorylation." Proc.Natl.Acad.Sci.USA, 111, E2937-E2946. doi: 10.1073/pnas.1406381111.

Abstract

Replication-dependent histone mRNAs end with a conserved stem loop that is recognized by stem-loop-binding protein (SLBP). The minimal RNA-processing domain of SLBP is phosphorylated at an internal threonine, and Drosophila SLBP (dSLBP) also is phosphorylated at four serines in its 18-aa C-terminal tail. We show that phosphorylation of dSLBP increases RNA-binding affinity dramatically, and we use structural and biophysical analyses of dSLBP and a crystal structure of human SLBP phosphorylated on the internal threonine to understand the striking improvement in RNA binding. Together these results suggest that, although the C-terminal tail of dSLBP does not contact the RNA, phosphorylation of the tail promotes SLBP conformations competent for RNA binding and thereby appears to reduce the entropic penalty for the association. Increased negative charge in this C-terminal tail balances positively charged residues, allowing a more compact ensemble of structures in the absence of RNA.