5f5v: Difference between revisions
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==Crystal structure of the Snu23-Prp38-MFAP1(217-296) complex of Chaetomium thermophilum== | |||
<StructureSection load='5f5v' size='340' side='right'caption='[[5f5v]], [[Resolution|resolution]] 3.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5f5v]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Chaetomium_thermophilum_var._thermophilum_DSM_1495 Chaetomium thermophilum var. thermophilum DSM 1495]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F5V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5F5V 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]] 3.1Å</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=5f5v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f5v OCA], [https://pdbe.org/5f5v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5f5v RCSB], [https://www.ebi.ac.uk/pdbsum/5f5v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5f5v ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/G0S1D3_CHATD G0S1D3_CHATD] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The spliceosomal B complex-specific protein Prp38 forms a complex with the intrinsically unstructured proteins MFAP1 and Snu23. Our binding and crystal structure analyses show that MFAP1 and Snu23 contact Prp38 via ER/K motif-stabilized single alpha helices, which have previously been recognized only as rigid connectors or force springs between protein domains. A variant of the Prp38-binding single alpha helix of MFAP1, in which ER/K motifs not involved in Prp38 binding were mutated, was less alpha-helical in isolation and showed a reduced Prp38 affinity, with opposing tendencies in interaction enthalpy and entropy. Our results indicate that the strengths of single alpha helix-based interactions can be tuned by the degree of helix stabilization in the unbound state. MFAP1, Snu23, and several other spliceosomal proteins contain multiple regions that likely form single alpha helices via which they might tether several binding partners and act as intermittent scaffolds that facilitate remodeling steps during assembly of an active spliceosome. | |||
Scaffolding in the Spliceosome via Single alpha Helices.,Ulrich AKC, Seeger M, Schutze T, Bartlick N, Wahl MC Structure. 2016 Nov 1;24(11):1972-1983. doi: 10.1016/j.str.2016.09.007. Epub 2016, Oct 20. PMID:27773687<ref>PMID:27773687</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Bartlick | <div class="pdbe-citations 5f5v" style="background-color:#fffaf0;"></div> | ||
[[Category: Seeger | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
</StructureSection> | |||
[[Category: Chaetomium thermophilum var. thermophilum DSM 1495]] | |||
[[Category: Large Structures]] | |||
[[Category: Bartlick N]] | |||
[[Category: Seeger M]] | |||
[[Category: Ulrich AKC]] | |||
[[Category: Wahl MC]] | |||
Latest revision as of 08:48, 12 July 2023
Crystal structure of the Snu23-Prp38-MFAP1(217-296) complex of Chaetomium thermophilum
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