1a0k
From Proteopedia
PROFILIN I FROM ARABIDOPSIS THALIANA
Structural highlights
FunctionPRF1_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 PubMedBACKGROUND: 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 AlsoReferences
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