4tux: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4tux]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TUX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TUX FirstGlance]. <br> | <table><tr><td colspan='2'>[[4tux]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TUX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TUX FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4tuw|4tuw]], [[4tv0|4tv0]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4tuw|4tuw]], [[4tv0|4tv0]]</td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4tux FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tux OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4tux RCSB], [http://www.ebi.ac.uk/pdbsum/4tux PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4tux FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tux OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4tux RCSB], [http://www.ebi.ac.uk/pdbsum/4tux PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/SLBP_DROME SLBP_DROME]] Involved in histone pre-mRNA 3' processing and couples histone mRNA production with the cell cycle. Both maternal and zygotic proteins play an essential and vital function for development.<ref>PMID:11157774</ref> <ref>PMID:19450530</ref> | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Zhang, J | [[Category: Zhang, J]] | ||
[[Category: Histone mrna stem-loop]] | [[Category: Histone mrna stem-loop]] | ||
[[Category: Rna binding protein-rna complex]] | [[Category: Rna binding protein-rna complex]] | ||
[[Category: Slbp]] | [[Category: Slbp]] | ||
Revision as of 19:32, 24 December 2014
drosophila stem-loop binding protein complexed with histone mRNA stem-loopdrosophila stem-loop binding protein complexed with histone mRNA stem-loop
Structural highlights
Function[SLBP_DROME] Involved in histone pre-mRNA 3' processing and couples histone mRNA production with the cell cycle. Both maternal and zygotic proteins play an essential and vital function for development.[1] [2] Publication Abstract from PubMedReplication-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. Molecular mechanisms for the regulation of histone mRNA stem-loop-binding protein by phosphorylation.,Zhang J, Tan D, DeRose EF, Perera L, Dominski Z, Marzluff WF, Tong L, Hall TM Proc Natl Acad Sci U S A. 2014 Jul 7. pii: 201406381. PMID:25002523[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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