4QOZ

Crystal structure of the histone mRNA stem-loop, stem-loop binding protein (phosphorylated), and 3'hExo ternary complex

Summary for 4QOZ

• Entry DOI: 10.2210/pdb4qoz/pdb
• Related: 4L8R
• Descriptor: histone mRNA stem-loop, 3'-5' exoribonuclease 1, Histone RNA hairpin-binding protein, ... (4 entities in total)
• Functional Keywords: histone mrna 3'-end processing, histone mrna translation, microrna homeostasis, 5.8s rrna 3'-end maturation, zfp100, lsm11, phosphorylation, nucleus, rna-hydrolase-rna binding protein complex, rna/hydrolase/rna binding protein
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm: Q8IV48 Q14493
• Total number of polymer chains: 5
• Total formula weight: 101292.06

Authors

Tan, D.,Tong, L. (deposition date: 2014-06-21, release date: 2014-07-23, Last modification date: 2024-10-16)

Primary citation

Zhang, J.,Tan, D.,DeRose, E.F.,Perera, L.,Dominski, Z.,Marzluff, W.F.,Tong, L.,Hall, T.M.
Molecular mechanisms for the regulation of histone mRNA stem-loop-binding protein by phosphorylation.
Proc.Natl.Acad.Sci.USA, 111:E2937-E2946, 2014

PubMed 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.

PubMed: 25002523
DOI: 10.1073/pnas.1406381111

Experimental method

X-RAY DIFFRACTION (2.304 Å)