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| | <StructureSection load='5ibw' size='340' side='right'caption='[[5ibw]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='5ibw' size='340' side='right'caption='[[5ibw]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5ibw]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Dicdi Dicdi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IBW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5IBW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5ibw]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IBW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IBW FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DDB_G0289563 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=44689 DICDI]), myoC, dmiC, DDB_G0276617 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=44689 DICDI])</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></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=5ibw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ibw OCA], [http://pdbe.org/5ibw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ibw RCSB], [http://www.ebi.ac.uk/pdbsum/5ibw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ibw ProSAT]</span></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=5ibw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ibw OCA], [https://pdbe.org/5ibw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ibw RCSB], [https://www.ebi.ac.uk/pdbsum/5ibw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ibw ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MYOC_DICDI MYOC_DICDI]] Myosin is a protein that binds to actin and has ATPase activity that is activated by actin. Involved in the process of phagocytosis and appears to support streaming behavior.<ref>PMID:8609164</ref> | + | [https://www.uniprot.org/uniprot/Q54HC2_DICDI Q54HC2_DICDI] |
| | <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: Dicdi]] | + | [[Category: Dictyostelium discoideum]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Langelaan, D N]] | + | [[Category: Langelaan DN]] |
| - | [[Category: Smith, S P]] | + | [[Category: Smith SP]] |
| - | [[Category: Motor protein]]
| + | |
| - | [[Category: Myosin iq motif complex]]
| + | |
| Structural highlights
Function
Q54HC2_DICDI
Publication Abstract from PubMed
Myosin light chains are key regulators of class 1 myosins and typically comprise two domains, with calmodulin being the archetypal example. They bind IQ motifs within the myosin neck region and amplify conformational changes in motor domain. A single lobe light chain, myosin light chain C (MlcC), was recently identified and shown to specifically bind to two sequentially divergent IQ motifs of the Dictyostelium myosin-1C. Towards providing a molecular basis of this interaction, the structures of apo-MlcC and a 2:1 MlcC:myosin-1C neck complex were determined. The two non-functional EF-hand motifs of MlcC pack together to form a globular four-helix bundle that opens up to expose a central hydrophobic groove, which interacts the N-terminal portion of the divergent IQ1 and IQ2 motifs. N- and C-terminal regions of MlcC make critical contacts that contribute to its specific interactions with the myosin-1C divergent IQ motifs; contacts that deviate from the traditional mode of calmodulin-IQ recognition.
Structure of the single-lobe myosin light chain C in complex with the light chain-binding domains of myosin-1C provides insights into divergent IQ-motif recognition.,Langelaan DN, Liburd J, Yang Y, Miller E, Chitayat S, Crawley SW, Cote GP, Smith SP J Biol Chem. 2016 Jul 27. pii: jbc.M116.746313. PMID:27466369[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Langelaan DN, Liburd J, Yang Y, Miller E, Chitayat S, Crawley SW, Cote GP, Smith SP. Structure of the single-lobe myosin light chain C in complex with the light chain-binding domains of myosin-1C provides insights into divergent IQ-motif recognition. J Biol Chem. 2016 Jul 27. pii: jbc.M116.746313. PMID:27466369 doi:http://dx.doi.org/10.1074/jbc.M116.746313
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