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| | <StructureSection load='6iqk' size='340' side='right'caption='[[6iqk]], [[Resolution|resolution]] 3.60Å' scene=''> | | <StructureSection load='6iqk' size='340' side='right'caption='[[6iqk]], [[Resolution|resolution]] 3.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6iqk]] is a 11 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IQK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6IQK FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6iqk]] is a 11 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IQK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6IQK FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</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]] 3.6Å</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=6iqk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6iqk OCA], [http://pdbe.org/6iqk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6iqk RCSB], [http://www.ebi.ac.uk/pdbsum/6iqk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6iqk 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=6iqk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6iqk OCA], [https://pdbe.org/6iqk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6iqk RCSB], [https://www.ebi.ac.uk/pdbsum/6iqk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6iqk ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PROF5_ARATH PROF5_ARATH]] Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG (By similarity). | + | [https://www.uniprot.org/uniprot/PRF3_ARATH PRF3_ARATH] Binds to actin monomers and regulates the organization of the actin cytoskeleton (PubMed:23052593, PubMed:29861135). Can increase the critical concentration (Cc) of actin assembly in vitro (PubMed:23052593). Acts as downstream effector of the hydrogen sulfide signaling to regulate the assembly and depolymerization of F-actin (PubMed:25652660). At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations (Probable). Binding to the poly-proline motif of formin induces oligomerization of PRF3 (PubMed:29861135). PRF3 oligomers inhibit formin-mediated actin assembly to modulate plant immunity triggered by pathogen-associated molecular patterns (PAMPs) (PubMed:29861135).<ref>PMID:23052593</ref> <ref>PMID:25652660</ref> <ref>PMID:29861135</ref> <ref>PMID:29861135</ref> |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | Profilins are abundant cytosolic proteins that are universally expressed in eukaryotes and regulate actin filament elongation by binding to both monomeric actin (G-actin) and formin proteins. The atypical profilin Arabidopsis AtPRF3 has been reported to cooperate with canonical profilin isoforms in suppressing formin-mediated actin polymerization during plant innate immunity responses. AtPRF3 has a 37-amino-acid-long N terminal extension (NTE), and its suppressive effect on actin assembly is derived from enhanced interaction with the poly-proline (Poly-P) of the formin AtFH1. However, the molecular mechanism remains unclear. Here, we solved the crystal structures of AtPRF3Delta22 and AtPRF3Delta37, as well as AtPRF2 apo form and in complex with AtFH1 Poly-P at 1.5-3.6 A resolutions. By combining these structures with molecular modeling, we found that AtPRF3Delta22 NTE has high plasticity, with a primary "closed" conformation that can adopt an open conformation that enables Poly-P binding. Furthermore, using molecular dynamics simulation and free-energy calculations of protein-protein binding, along with experimental validation, we show that the AtPRF3Delta22 binds to Poly-P in an adaptive manner, thereby enabling different binding modes that maintain the interaction through disordered sequences. Together, our structural and simulation results suggest that the dynamic conformational changes of the AtPRF3 NTE upon Poly-P binding modulate their interactions to fine-tune formin-mediated actin assembly.
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| | | | |
| - | Structural and computational examination of the Arabidopsis profilin-Poly-P complex reveals mechanistic details in profilin-regulated actin assembly.,Qiao Z, Sun H, Ng JTY, Ma Q, Koh SH, Mu Y, Miao Y, Gao YG J Biol Chem. 2019 Oct 25. pii: RA119.011307. doi: 10.1074/jbc.RA119.011307. PMID:31653702<ref>PMID:31653702</ref>
| + | ==See Also== |
| - | | + | *[[Profilin 3D Structures|Profilin 3D Structures]] |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 6iqk" style="background-color:#fffaf0;"></div>
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| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Arabidopsis thaliana]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Gao, Y]] | + | [[Category: Gao Y]] |
| - | [[Category: Qiao, Z]] | + | [[Category: Qiao Z]] |
| - | [[Category: Actin binding]]
| + | |
| - | [[Category: Plant protein]]
| + | |
| - | [[Category: Regulate actin network]]
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| Structural highlights
Function
PRF3_ARATH Binds to actin monomers and regulates the organization of the actin cytoskeleton (PubMed:23052593, PubMed:29861135). Can increase the critical concentration (Cc) of actin assembly in vitro (PubMed:23052593). Acts as downstream effector of the hydrogen sulfide signaling to regulate the assembly and depolymerization of F-actin (PubMed:25652660). At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations (Probable). Binding to the poly-proline motif of formin induces oligomerization of PRF3 (PubMed:29861135). PRF3 oligomers inhibit formin-mediated actin assembly to modulate plant immunity triggered by pathogen-associated molecular patterns (PAMPs) (PubMed:29861135).[1] [2] [3] [4]
See Also
References
- ↑ Fan T, Zhai H, Shi W, Wang J, Jia H, Xiang Y, An L. Overexpression of profilin 3 affects cell elongation and F-actin organization in Arabidopsis thaliana. Plant Cell Rep. 2013 Jan;32(1):149-60. PMID:23052593 doi:10.1007/s00299-012-1349-2
- ↑ Jia H, Hu Y, Fan T, Li J. Hydrogen sulfide modulates actin-dependent auxin transport via regulating ABPs results in changing of root development in Arabidopsis. Sci Rep. 2015 Feb 5;5:8251. PMID:25652660 doi:10.1038/srep08251
- ↑ Sun H, Qiao Z, Chua KP, Tursic A, Liu X, Gao YG, Mu Y, Hou X, Miao Y. Profilin Negatively Regulates Formin-Mediated Actin Assembly to Modulate PAMP-Triggered Plant Immunity. Curr Biol. 2018 Jun 18;28(12):1882-1895.e7. PMID:29861135 doi:10.1016/j.cub.2018.04.045
- ↑ Sun H, Qiao Z, Chua KP, Tursic A, Liu X, Gao YG, Mu Y, Hou X, Miao Y. Profilin Negatively Regulates Formin-Mediated Actin Assembly to Modulate PAMP-Triggered Plant Immunity. Curr Biol. 2018 Jun 18;28(12):1882-1895.e7. PMID:29861135 doi:10.1016/j.cub.2018.04.045
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