2xz2: Difference between revisions
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New page: '''Unreleased structure''' The entry 2xz2 is ON HOLD Authors: Moreno-Morcillo, M., Fribourg, S. Description: Crystal structure of CstF-50 homodimerization domain ''Page seeded by [htt... |
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The | ==Crystal structure of CstF-50 homodimerization domain== | ||
<StructureSection load='2xz2' size='340' side='right'caption='[[2xz2]], [[Resolution|resolution]] 1.40Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2xz2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XZ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XZ2 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2xz2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xz2 OCA], [https://pdbe.org/2xz2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xz2 RCSB], [https://www.ebi.ac.uk/pdbsum/2xz2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xz2 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The Cleavage stimulation Factor (CstF) complex is composed of three subunits and is essential for pre-mRNA 3'-end processing. CstF recognizes U and G/U-rich cis-acting RNA sequence elements and helps stabilize the Cleavage and Polyadenylation Specificity Factor (CPSF) at the polyadenylation site as required for productive RNA cleavage. Here, we describe the crystal structure of the N-terminal domain of Drosophila CstF-50 subunit. It forms a compact homodimer that exposes two geometrically opposite, identical, and conserved surfaces that may serve as binding platform. Together with previous data on the structure of CstF-77, homodimerization of CstF-50 N-terminal domain supports the model in which the functional state of CstF is a heterohexamer. | |||
Hexameric architecture of CstF supported by CstF-50 homodimerization domain structure.,Moreno-Morcillo M, Minvielle-Sebastia L, Mackereth C, Fribourg S RNA. 2011 Jan 13. PMID:21233223<ref>PMID:21233223</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2xz2" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Drosophila melanogaster]] | |||
[[Category: Large Structures]] | |||
[[Category: Fribourg S]] | |||
[[Category: Moreno-Morcillo M]] | |||
Latest revision as of 17:01, 1 February 2024
Crystal structure of CstF-50 homodimerization domainCrystal structure of CstF-50 homodimerization domain
Structural highlights
Publication Abstract from PubMedThe Cleavage stimulation Factor (CstF) complex is composed of three subunits and is essential for pre-mRNA 3'-end processing. CstF recognizes U and G/U-rich cis-acting RNA sequence elements and helps stabilize the Cleavage and Polyadenylation Specificity Factor (CPSF) at the polyadenylation site as required for productive RNA cleavage. Here, we describe the crystal structure of the N-terminal domain of Drosophila CstF-50 subunit. It forms a compact homodimer that exposes two geometrically opposite, identical, and conserved surfaces that may serve as binding platform. Together with previous data on the structure of CstF-77, homodimerization of CstF-50 N-terminal domain supports the model in which the functional state of CstF is a heterohexamer. Hexameric architecture of CstF supported by CstF-50 homodimerization domain structure.,Moreno-Morcillo M, Minvielle-Sebastia L, Mackereth C, Fribourg S RNA. 2011 Jan 13. PMID:21233223[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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