PDBsum entry 4tuw

RNA binding protein/RNA

PDB id: 4tuw

Contents

Protein chains

71 a.a.

70 a.a.

DNA/RNA

Metals

_CA ×5

PDB id:

4tuw

Name:

RNA binding protein/RNA

Title:

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

Structure:

Histone RNA hairpin-binding protein. Chain: a, b. Fragment: unp residues 184-276. Synonym: histone stem-loop-binding protein. Engineered: yes. Mutation: yes. Histone mRNA 3' stem loop. Chain: d. Engineered: yes.

Source:

Drosophila melanogaster. Fruit fly. Organism_taxid: 7227. Gene: slbp, cg11886. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Synthetic construct. Organism_taxid: 32630.

Resolution:

2.90Å R-factor: 0.219 R-free: 0.263

Authors:

J.Zhang

Key ref:

J.Zhang et al. (2014). Molecular mechanisms for the regulation of histone mRNA stem-loop-binding protein by phosphorylation. Proc Natl Acad Sci U S A, 111, E2937. PubMed id: 25002523 DOI: 10.1073/pnas.1406381111

Date:

25-Jun-14 Release date: 23-Jul-14

Protein chain

Q9VAN6  (SLBP_DROME) -  Histone RNA hairpin-binding protein from Drosophila melanogaster

Seq: 276 a.a.

Struc: 71 a.a.*

Protein chain

Q9VAN6  (SLBP_DROME) -  Histone RNA hairpin-binding protein from Drosophila melanogaster

Seq: 276 a.a.

Struc: 70 a.a.*

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

DNA/RNA chains

G-G-C-C-A-A-A-G-G-C-C-C-U-U-U-U-C-A-G-G-G-C-C-A-C-C 26 bases

G-G-C-C-A-A-A-G-G-C-C-C-U-U-U-U-C-A-G-G-G-C-C-A-C-C-C-C 28 bases

DOI no: 10.1073/pnas.1406381111

Proc Natl Acad Sci U S A 111:E2937 (2014)

PubMed id: 25002523

Molecular mechanisms for the regulation of histone mRNA stem-loop-binding protein by phosphorylation.

J.Zhang, D.Tan, E.F.DeRose, L.Perera, Z.Dominski, W.F.Marzluff, L.Tong, T.M.Hall.

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.