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[[Image:1a0k.gif|left|200px]]
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{{STRUCTURE_1a0k|  PDB=1a0k  |  SCENE=  }}
'''PROFILIN I FROM ARABIDOPSIS THALIANA'''


==PROFILIN I FROM ARABIDOPSIS THALIANA==
<StructureSection load='1a0k' size='340' side='right'caption='[[1a0k]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1a0k]] is a 1 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=1A0K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A0K FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#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=1a0k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a0k OCA], [https://pdbe.org/1a0k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a0k RCSB], [https://www.ebi.ac.uk/pdbsum/1a0k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a0k ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PRF1_ARATH PRF1_ARATH] Binds to actin monomers and regulates the organization of the actin cytoskeleton (PubMed:26574597). At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations (PubMed:29861135). At low concentrations, associates with the poly-proline motif of formins to enhance actin filament elongation rate (PubMed:29861135). Binds ACT1, ACT7 and ACT11 and inhibits actin polymerization (PubMed:26578694). Coordinates the stochastic dynamic properties of actin filaments by modulating formin-mediated actin nucleation and assembly during axial cell expansion (PubMed:26574597). Binds G-actin and poly-L-proline in vitro (PubMed:19200149). 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).<ref>PMID:19200149</ref> <ref>PMID:26574597</ref> <ref>PMID:26578694</ref> <ref>PMID:29861135</ref> <ref>PMID:30056100</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a0/1a0k_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1a0k ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
BACKGROUND: Profilins are small eukaryotic proteins involved in modulating the assembly of actin microfilaments in the cytoplasm. They are able to bind both phosphatidylinositol-4,5-bisphosphate and poly-L-proline (PLP) and thus play a critical role in signaling pathways. Plant profilins are of interest because immunological cross-reactivity between pollen and human profilin may be the cause of hay fever and broad allergies to pollens. RESULTS: The determination of the Arabidopsis thaliana profilin isoform I structure, using multiwavelength anomalous diffraction (MAD) to obtain structure-factor phases, is reported here. The structure of Arabidopsis profilin is similar to that of previously determined profilin structures. Conserved amino acid residues in profilins from plants, mammals, and lower eukaryotes are critically important in dictating the geometry of the PLP-binding site and the overall polypeptide fold. The main feature distinguishing plant profilins from other profilins is a solvent-filled pocket located in the most variable region of the fold. CONCLUSIONS: Comparison of the structures of SH3 domains with those of profilins from three distinct sources suggests that the mode of PLP binding may be similar. A comparison of three profilin structures from different families reveals only partial conservation of the actin-binding surface. The proximity of the semi-conserved actin-binding site and the binding pocket characteristic of plant profilins suggests that epitopes encompassing both features are responsible for the cross-reactivity of antibodies between human and plant profilins thought to be responsible for type I allergies.


==Overview==
The crystal structure of a major allergen from plants.,Thorn KS, Christensen HE, Shigeta R, Huddler D, Shalaby L, Lindberg U, Chua NH, Schutt CE Structure. 1997 Jan 15;5(1):19-32. PMID:9016723<ref>PMID:9016723</ref>
BACKGROUND: Profilins are small eukaryotic proteins involved in modulating the assembly of actin microfilaments in the cytoplasm. They are able to bind both phosphatidylinositol-4,5-bisphosphate and poly-L-proline (PLP) and thus play a critical role in signaling pathways. Plant profilins are of interest because immunological cross-reactivity between pollen and human profilin may be the cause of hay fever and broad allergies to pollens. RESULTS: The determination of the Arabidopsis thaliana profilin isoform I structure, using multiwavelength anomalous diffraction (MAD) to obtain structure-factor phases, is reported here. The structure of Arabidopsis profilin is similar to that of previously determined profilin structures. Conserved amino acid residues in profilins from plants, mammals, and lower eukaryotes are critically important in dictating the geometry of the PLP-binding site and the overall polypeptide fold. The main feature distinguishing plant profilins from other profilins is a solvent-filled pocket located in the most variable region of the fold. CONCLUSIONS: Comparison of the structures of SH3 domains with those of profilins from three distinct sources suggests that the mode of PLP binding may be similar. A comparison of three profilin structures from different families reveals only partial conservation of the actin-binding surface. The proximity of the semi-conserved actin-binding site and the binding pocket characteristic of plant profilins suggests that epitopes encompassing both features are responsible for the cross-reactivity of antibodies between human and plant profilins thought to be responsible for type I allergies.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1A0K is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A0K OCA].
</div>
<div class="pdbe-citations 1a0k" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
The crystal structure of a major allergen from plants., Thorn KS, Christensen HE, Shigeta R, Huddler D, Shalaby L, Lindberg U, Chua NH, Schutt CE, Structure. 1997 Jan 15;5(1):19-32. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9016723 9016723]
*[[Profilin 3D Structures|Profilin 3D Structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Arabidopsis thaliana]]
[[Category: Arabidopsis thaliana]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Huddler, D.]]
[[Category: Huddler D]]
[[Category: Junior, R Shigeta.]]
[[Category: Lindberg U]]
[[Category: Lindberg, U.]]
[[Category: Schutt CE]]
[[Category: Schutt, C E.]]
[[Category: Shigeta Junior R]]
[[Category: Actin-binding]]
[[Category: Cytoskeleton]]
[[Category: Profilin]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 09:37:55 2008''

Latest revision as of 13:43, 2 August 2023

PROFILIN I FROM ARABIDOPSIS THALIANAPROFILIN I FROM ARABIDOPSIS THALIANA

Structural highlights

1a0k is a 1 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 2.2Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PRF1_ARATH Binds to actin monomers and regulates the organization of the actin cytoskeleton (PubMed:26574597). At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations (PubMed:29861135). At low concentrations, associates with the poly-proline motif of formins to enhance actin filament elongation rate (PubMed:29861135). Binds ACT1, ACT7 and ACT11 and inhibits actin polymerization (PubMed:26578694). Coordinates the stochastic dynamic properties of actin filaments by modulating formin-mediated actin nucleation and assembly during axial cell expansion (PubMed:26574597). Binds G-actin and poly-L-proline in vitro (PubMed:19200149). 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).[1] [2] [3] [4] [5]

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

BACKGROUND: Profilins are small eukaryotic proteins involved in modulating the assembly of actin microfilaments in the cytoplasm. They are able to bind both phosphatidylinositol-4,5-bisphosphate and poly-L-proline (PLP) and thus play a critical role in signaling pathways. Plant profilins are of interest because immunological cross-reactivity between pollen and human profilin may be the cause of hay fever and broad allergies to pollens. RESULTS: The determination of the Arabidopsis thaliana profilin isoform I structure, using multiwavelength anomalous diffraction (MAD) to obtain structure-factor phases, is reported here. The structure of Arabidopsis profilin is similar to that of previously determined profilin structures. Conserved amino acid residues in profilins from plants, mammals, and lower eukaryotes are critically important in dictating the geometry of the PLP-binding site and the overall polypeptide fold. The main feature distinguishing plant profilins from other profilins is a solvent-filled pocket located in the most variable region of the fold. CONCLUSIONS: Comparison of the structures of SH3 domains with those of profilins from three distinct sources suggests that the mode of PLP binding may be similar. A comparison of three profilin structures from different families reveals only partial conservation of the actin-binding surface. The proximity of the semi-conserved actin-binding site and the binding pocket characteristic of plant profilins suggests that epitopes encompassing both features are responsible for the cross-reactivity of antibodies between human and plant profilins thought to be responsible for type I allergies.

The crystal structure of a major allergen from plants.,Thorn KS, Christensen HE, Shigeta R, Huddler D, Shalaby L, Lindberg U, Chua NH, Schutt CE Structure. 1997 Jan 15;5(1):19-32. PMID:9016723[6]

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

See Also

References

  1. ↑ 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
  2. ↑ Cao L, Henty-Ridilla JL, Blanchoin L, Staiger CJ. Profilin-Dependent Nucleation and Assembly of Actin Filaments Controls Cell Elongation in Arabidopsis. Plant Physiol. 2016 Jan;170(1):220-33. PMID:26574597 doi:10.1104/pp.15.01321
  3. ↑ 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
  4. ↑ 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
  5. ↑ 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
  6. ↑ Thorn KS, Christensen HE, Shigeta R, Huddler D, Shalaby L, Lindberg U, Chua NH, Schutt CE. The crystal structure of a major allergen from plants. Structure. 1997 Jan 15;5(1):19-32. PMID:9016723

1a0k, resolution 2.20Å

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