6ljd: Difference between revisions
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==Crystal structure of fragmin F2-F3 domains (calcium condition)== | |||
<StructureSection load='6ljd' size='340' side='right'caption='[[6ljd]], [[Resolution|resolution]] 2.15Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6ljd]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LJD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6LJD FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=6ljd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ljd OCA], [http://pdbe.org/6ljd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ljd RCSB], [http://www.ebi.ac.uk/pdbsum/6ljd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ljd ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Gelsolin superfamily proteins, consisting of multiple domains (usually six), sever actin filaments and cap the barbed ends in a Ca(2+)-dependent manner. Two types of evolutionally conserved Ca(2+)-binding sites have been identified in this family; type-1 (between gelsolin and actin) and type-2 (within the gelsolin domain). Fragmin, a member in the slime mold Physarum polycephalum, consists of three domains (F1-F3) that are highly similar to the N-terminal half of mammalian gelsolin (G1-G3). Despite their similarities, the two proteins exhibit a significant difference in the Ca(2+) dependency; F1-F3 absolutely requires Ca(2+) for the filament severing whereas G1-G3 does not. In this study, we examined the strong dependency of fragmin on Ca(2+) using biochemical and structural approaches. Our co-sedimentation assay demonstrated that Ca(2+) significantly enhanced the binding of F2-F3 to actin. We determined the crystal structure of F2-F3 in the presence of Ca(2+). F2-F3 binds a total of three calcium ions; while two are located in type-2 sites within F2 or F3, the remaining one resides between the F2 long helix and the F3 short helix. The inter-domain Ca(2+)-coordination appears to stabilize F2-F3 in a closely packed configuration. Notably, the F3 long helix exhibits a bent conformation which is different from the straight G3 long helix in the presence of Ca(2+). Our results provide the first structural evidence for the existence of an unconventional Ca(2+)-binding site in the gelsolin superfamily proteins. | |||
Novel inter-domain Ca(2+)-binding site in the gelsolin superfamily protein fragmin.,Takeda S, Fujiwara I, Sugimoto Y, Oda T, Narita A, Maeda Y J Muscle Res Cell Motil. 2019 Dec 20. pii: 10.1007/s10974-019-09571-5. doi:, 10.1007/s10974-019-09571-5. PMID:31863323<ref>PMID:31863323</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6ljd" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Takeda, S]] | |||
[[Category: Actin filament severing]] | |||
[[Category: Calcium regulation]] | |||
[[Category: Cytosolic protein]] | |||
[[Category: Fragmin]] | |||
[[Category: Gelsolin family protein]] | |||
