Summary information and primary citation

4qoz; DSSR-derived features in text and JSON formats
RNA-hydrolase-RNA binding protein
X-ray (2.304 Å)
Crystal structure of the histone mrna stem-loop, stem-loop binding protein (phosphorylated), and 3'hexo ternary complex
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.
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.

Cartoon-block schematics in six views (download the tarball)

PyMOL session file Download PDB file View in 3Dmol.js