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| | ==Solution structure of Coactosin-like protein (Cofilin family) from Mus Musculus== | | ==Solution structure of Coactosin-like protein (Cofilin family) from Mus Musculus== |
| - | <StructureSection load='1udm' size='340' side='right'caption='[[1udm]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='1udm' size='340' side='right'caption='[[1udm]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1udm]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UDM OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1UDM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1udm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UDM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UDM FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RIKEN cDNA 2010004C08 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1udm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1udm OCA], [http://pdbe.org/1udm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1udm RCSB], [http://www.ebi.ac.uk/pdbsum/1udm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1udm ProSAT], [http://www.topsan.org/Proteins/RSGI/1udm TOPSAN]</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=1udm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1udm OCA], [https://pdbe.org/1udm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1udm RCSB], [https://www.ebi.ac.uk/pdbsum/1udm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1udm ProSAT], [https://www.topsan.org/Proteins/RSGI/1udm TOPSAN]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/COAC_MOUSE COAC_MOUSE]] Necessary for the biosynthesis of coenzyme A. Catalyzes the decarboxylation of 4-phosphopantothenoylcysteine to form 4'-phosphopantotheine (By similarity). | + | [https://www.uniprot.org/uniprot/COTL1_MOUSE COTL1_MOUSE] Binds to F-actin in a calcium-independent manner. Has no direct effect on actin depolymerization.<ref>PMID:11785969</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: Goroncy, A K]] | + | [[Category: Goroncy AK]] |
| - | [[Category: Inoue, M]] | + | [[Category: Inoue M]] |
| - | [[Category: Kigawa, T]] | + | [[Category: Kigawa T]] |
| - | [[Category: Kobayashi, N]] | + | [[Category: Kobayashi N]] |
| - | [[Category: Koshiba, S]] | + | [[Category: Koshiba S]] |
| - | [[Category: Structural genomic]]
| + | [[Category: Tochio N]] |
| - | [[Category: Tochio, N]] | + | [[Category: Yokoyama S]] |
| - | [[Category: Yokoyama, S]] | + | |
| - | [[Category: Actin binding protein]]
| + | |
| - | [[Category: Cytoskeletal]]
| + | |
| - | [[Category: Protein binding]]
| + | |
| - | [[Category: Rsgi]]
| + | |
| Structural highlights
Function
COTL1_MOUSE Binds to F-actin in a calcium-independent manner. Has no direct effect on actin depolymerization.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Actin is one of the most conserved proteins in nature. Its assembly and disassembly are regulated by many proteins, including the family of actin-depolymerizing factor homology (ADF-H) domains. ADF-H domains can be divided into five classes: ADF/cofilin, glia maturation factor (GMF), coactosin, twinfilin, and Abp1/drebrin. The best-characterized class is ADF/cofilin. The other four classes have drawn much less attention and very few structures have been reported. This study presents the solution NMR structure of the ADF-H domain of human HIP-55-drebrin-like protein, the first published structure of a drebrin-like domain (mammalian), and the first published structure of GMF beta (mouse). We also determined the structures of mouse GMF gamma, the mouse coactosin-like domain and the C-terminal ADF-H domain of mouse twinfilin 1. Although the overall fold of the five domains is similar, some significant differences provide valuable insights into filamentous actin (F-actin) and globular actin (G-actin) binding, including the identification of binding residues on the long central helix. This long helix is stabilized by three or four residues. Notably, the F-actin binding sites of mouse GMF beta and GMF gamma contain two additional beta-strands not seen in other ADF-H structures. The G-actin binding site of the ADF-H domain of human HIP-55-drebrin-like protein is absent and distorted in mouse GMF beta and GMF gamma.
NMR solution structures of actin depolymerizing factor homology domains.,Goroncy AK, Koshiba S, Tochio N, Tomizawa T, Sato M, Inoue M, Watanabe S, Hayashizaki Y, Tanaka A, Kigawa T, Yokoyama S Protein Sci. 2009 Nov;18(11):2384-92. PMID:19768801[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Doucet J, Provost P, Samuelsson B, Radmark O. Molecular cloning and functional characterization of mouse coactosin-like protein. Biochem Biophys Res Commun. 2002 Jan 18;290(2):783-9. PMID:11785969 doi:http://dx.doi.org/10.1006/bbrc.2001.6236
- ↑ Goroncy AK, Koshiba S, Tochio N, Tomizawa T, Sato M, Inoue M, Watanabe S, Hayashizaki Y, Tanaka A, Kigawa T, Yokoyama S. NMR solution structures of actin depolymerizing factor homology domains. Protein Sci. 2009 Nov;18(11):2384-92. PMID:19768801 doi:10.1002/pro.248
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