6iqi

From Proteopedia

(Difference between revisions)

Current revision

crystal structure of Arabidopsis thaliana Profilin 2

Structural highlights

6iqi is a 2 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.4Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PRF2_ARATH Binds to actin monomers and regulates the organization of the actin cytoskeleton (PubMed:21090759). At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations (PubMed:26996265, PubMed:16313636, PubMed:29861135). At low concentrations, associates with the poly-proline motif of formins to enhance actin filament elongation rate (PubMed:29861135). Binds G-actin and poly-L-proline with low affinity in vitro (PubMed:19200149). Binds ACT1, ACT7 and ACT11 and inhibits actin polymerization (PubMed:26578694). May be involved in the cross-talk between vesicular trafficking and the actin cytoskeleton (PubMed:21090759). At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations (By similarity). Inhibits cell growth of various pathogenic fungal strains (PubMed:30056100). May play a role as antifungal proteins in the defense system against fungal pathogen attacks (PubMed:30056100).[UniProtKB:P07737]^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7]

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.

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^[8]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Deeks MJ, Cvrcková F, Machesky LM, Mikitová V, Ketelaar T, Zársky V, Davies B, Hussey PJ. Arabidopsis group Ie formins localize to specific cell membrane domains, interact with actin-binding proteins and cause defects in cell expansion upon aberrant expression. New Phytol. 2005 Dec;168(3):529-40. PMID:16313636 doi:10.1111/j.1469-8137.2005.01582.x
↑ Wang F, Jing Y, Wang Z, Mao T, Samaj J, Yuan M, Ren H. Arabidopsis profilin isoforms, PRF1 and PRF2 show distinctive binding activities and subcellular distributions. J Integr Plant Biol. 2009 Feb;51(2):113-21. PMID:19200149 doi:10.1111/j.1744-7909.2008.00781.x
↑ Takác T, Pechan T, Richter H, Müller J, Eck C, Böhm N, Obert B, Ren H, Niehaus K, Samaj J. Proteomics on brefeldin A-treated Arabidopsis roots reveals profilin 2 as a new protein involved in the cross-talk between vesicular trafficking and the actin cytoskeleton. J Proteome Res. 2011 Feb 4;10(2):488-501. PMID:21090759 doi:10.1021/pr100690f
↑ Kijima ST, Hirose K, Kong SG, Wada M, Uyeda TQ. Distinct Biochemical Properties of Arabidopsis thaliana Actin Isoforms. Plant Cell Physiol. 2016 Jan;57(1):46-56. PMID:26578694 doi:10.1093/pcp/pcv176
↑ Zhang S, Liu C, Wang J, Ren Z, Staiger CJ, Ren H. A Processive Arabidopsis Formin Modulates Actin Filament Dynamics in Association with Profilin. Mol Plant. 2016 Jun 6;9(6):900-10. PMID:26996265 doi:10.1016/j.molp.2016.03.006
↑ 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
↑ Park SC, Kim IR, Kim JY, Lee Y, Kim EJ, Jung JH, Jung YJ, Jang MK, Lee JR. Molecular mechanism of Arabidopsis thaliana profilins as antifungal proteins. Biochim Biophys Acta Gen Subj. 2018 Dec;1862(12):2545-2554. PMID:30056100 doi:10.1016/j.bbagen.2018.07.028
↑ Qiao Z, Sun H, Ng JTY, Ma Q, Koh SH, Mu Y, Miao Y, Gao YG. Structural and computational examination of the Arabidopsis profilin-Poly-P complex reveals mechanistic details in profilin-regulated actin assembly. J Biol Chem. 2019 Oct 25. pii: RA119.011307. doi: 10.1074/jbc.RA119.011307. PMID:31653702 doi:http://dx.doi.org/10.1074/jbc.RA119.011307

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6iqi"

Categories: Arabidopsis thaliana | Large Structures | Gao Y | Qiao Z

@@ Line 3: / Line 3: @@
 <StructureSection load='6iqi' size='340' side='right'caption='[[6iqi]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6iqi]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IQI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6IQI FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6iqi]] is a 2 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=6IQI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6IQI FirstGlance]. <br>
-</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=6iqi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6iqi OCA], [http://pdbe.org/6iqi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6iqi RCSB], [http://www.ebi.ac.uk/pdbsum/6iqi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6iqi ProSAT]</span></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]] 2.4&#8491;</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=6iqi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6iqi OCA], [https://pdbe.org/6iqi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6iqi RCSB], [https://www.ebi.ac.uk/pdbsum/6iqi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6iqi ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/PROF2_ARATH PROF2_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/PRF2_ARATH PRF2_ARATH] Binds to actin monomers and regulates the organization of the actin cytoskeleton (PubMed:21090759). At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations (PubMed:26996265, PubMed:16313636, PubMed:29861135). At low concentrations, associates with the poly-proline motif of formins to enhance actin filament elongation rate (PubMed:29861135). Binds G-actin and poly-L-proline with low affinity in vitro (PubMed:19200149). Binds ACT1, ACT7 and ACT11 and inhibits actin polymerization (PubMed:26578694). May be involved in the cross-talk between vesicular trafficking and the actin cytoskeleton (PubMed:21090759). At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations (By similarity). Inhibits cell growth of various pathogenic fungal strains (PubMed:30056100). May play a role as antifungal proteins in the defense system against fungal pathogen attacks (PubMed:30056100).[UniProtKB:P07737]<ref>PMID:16313636</ref> <ref>PMID:19200149</ref> <ref>PMID:21090759</ref> <ref>PMID:26578694</ref> <ref>PMID:26996265</ref> <ref>PMID:29861135</ref> <ref>PMID:30056100</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 17: / Line 18: @@
 </div>
 <div class="pdbe-citations 6iqi" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Profilin 3D Structures|Profilin 3D Structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Arabidopsis thaliana]]
 [[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]]

6iqi

From Proteopedia

Current revision

crystal structure of Arabidopsis thaliana Profilin 2

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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