PDBsum entry 1a0k

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protein links
Cytoskeleton PDB id
Protein chain
130 a.a. *
Waters ×78
* Residue conservation analysis
PDB id:
Name: Cytoskeleton
Title: Profilin i from arabidopsis thaliana
Structure: Profilin. Chain: a. Engineered: yes
Source: Arabidopsis thaliana. Thale cress. Organism_taxid: 3702. Strain: columbia. Cell_line: bl21. Cellular_location: cellular cytoskeleton. Gene: pfn. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
2.20Å     R-factor:   0.172     R-free:   0.238
Authors: R.Shigeta Junior,D.Huddler,U.Lindberg,C.E.Schutt
Key ref:
K.S.Thorn et al. (1997). The crystal structure of a major allergen from plants. Structure, 5, 19-32. PubMed id: 9016723 DOI: 10.1016/S0969-2126(97)00163-9
02-Dec-97     Release date:   18-Mar-98    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
Q42449  (PROF1_ARATH) -  Profilin-1
131 a.a.
130 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     apoplast   11 terms 
  Biological process     unidimensional cell growth   4 terms 
  Biochemical function     actin binding     1 term  


DOI no: 10.1016/S0969-2126(97)00163-9 Structure 5:19-32 (1997)
PubMed id: 9016723  
The crystal structure of a major allergen from plants.
K.S.Thorn, H.E.Christensen, R.Shigeta, D.Huddler, L.Shalaby, U.Lindberg, N.H.Chua, C.E.Schutt.
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.
  Selected figure(s)  
Figure 4.
Figure 4. Stereo view showing the water mediated contact between b strands 1 and 7 of Arabidopsis profilin. The water molecule is hydrogen bonded to the amide of Asp 107 and the carbonyl of His 19 and is further stabilized by a hydrogen bond to the sidechain of residue Thr21; hydrogen bonds are shown as dashed lines. All residue numbers are in Arabidopsis sequence numbering. (Figure generated using the program MOLSCRIPT [69].)
  The above figure is reprinted by permission from Cell Press: Structure (1997, 5, 19-32) copyright 1997.  
  Figure was selected by the author.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21086179 A.Amini, M.Sankian, M.A.Assarehzadegan, F.Vahedi, and A.Varasteh (2011).
Chenopodium album pollen profilin (Che a 2): homology modeling and evaluation of cross-reactivity with allergenic profilins based on predicted potential IgE epitopes and IgE reactivity analysis.
  Mol Biol Rep, 38, 2579-2587.  
20205701 L.Tordesillas, L.F.Pacios, A.Palacín, J.Cuesta-Herranz, M.Madero, and A.Díaz-Perales (2010).
Characterization of IgE epitopes of Cuc m 2, the major melon allergen, and their role in cross-reactivity with pollen profilins.
  Clin Exp Allergy, 40, 174-181.  
20622444 M.A.Assarehzadegan, A.Amini, M.Sankian, M.Tehrani, F.Jabbari, and A.Varasteh (2010).
Sal k 4, a new allergen of Salsola kali, is profilin: a predictive value of conserved conformational regions in cross-reactivity with other plant-derived profilins.
  Biosci Biotechnol Biochem, 74, 1441-1446.  
19307716 J.A.Doebbler, and R.B.Von Dreele (2009).
Application of molecular replacement to protein powder data from image plates.
  Acta Crystallogr D Biol Crystallogr, 65, 348-355.  
19000816 I.Kursula, P.Kursula, M.Ganter, S.Panjikar, K.Matuschewski, and H.Schüler (2008).
Structural basis for parasite-specific functions of the divergent profilin of Plasmodium falciparum.
  Structure, 16, 1638-1648.
PDB codes: 2jkf 2jkg
17397911 G.López-Torrejón, A.Díaz-Perales, J.Rodríguez, R.Sánchez-Monge, J.F.Crespo, G.Salcedo, and L.F.Pacios (2007).
An experimental and modeling-based approach to locate IgE epitopes of plant profilin allergens.
  J Allergy Clin Immunol, 119, 1481-1488.  
16317718 D.Polet, A.Lambrechts, K.Ono, A.Mah, F.Peelman, J.Vandekerckhove, D.L.Baillie, C.Ampe, and S.Ono (2006).
Caenorhabditis elegans expresses three functional profilins in a tissue-specific manner.
  Cell Motil Cytoskeleton, 63, 14-28.  
17010111 M.Abu-Abied, L.Golomb, E.Belausov, S.Huang, B.Geiger, Z.Kam, C.J.Staiger, and E.Sadot (2006).
Identification of plant cytoskeleton-interacting proteins by screening for actin stress fiber association in mammalian fibroblasts.
  Plant J, 48, 367-379.  
16827923 R.Aparicio-Fabre, G.Guillén, G.Estrada, J.Olivares-Grajales, G.Gurrola, and F.Sánchez (2006).
Profilin tyrosine phosphorylation in poly-L-proline-binding regions inhibits binding to phosphoinositide 3-kinase in Phaseolus vulgaris.
  Plant J, 47, 491-500.  
15880548 L.J.Ball, R.Kühne, J.Schneider-Mergener, and H.Oschkinat (2005).
Recognition of Proline-Rich Motifs by Protein-Protein-Interaction Domains.
  Angew Chem Int Ed Engl, 44, 2852-2869.  
16153305 M.Sankian, A.Varasteh, N.Pazouki, and M.Mahmoudi (2005).
Sequence homology: a poor predictive value for profilins cross-reactivity.
  Clin Mol Allergy, 3, 13.  
12169172 A.Nieto, A.Mazón, M.Boquete, F.Carballada, J.A.Asturias, J.Martínez, and A.Martínez (2002).
Assessment of profilin as an allergen for latex-sensitized patients.
  Allergy, 57, 776-784.  
12077438 K.Rajashankar, A.Bufe, W.Weber, S.Eschenburg, B.Lindner, and C.Betzel (2002).
Structure of the functional domain of the major grass-pollen allergen Phlp 5b.
  Acta Crystallogr D Biol Crystallogr, 58, 1175-1181.
PDB code: 1l3p
11732068 D.W.McCurdy, D.R.Kovar, and C.J.Staiger (2001).
Actin and actin-binding proteins in higher plants.
  Protoplasma, 215, 89.  
10848918 S.Scheurer, A.Wangorsch, D.Haustein, and S.Vieths (2000).
Cloning of the minor allergen Api g 4 profilin from celery (Apium graveolens) and its cross-reactivity with birch pollen profilin Bet v 2.
  Clin Exp Allergy, 30, 962-971.  
11032796 Y.S.Ho, L.M.Burden, and J.H.Hurley (2000).
Structure of the GAF domain, a ubiquitous signaling motif and a new class of cyclic GMP receptor.
  EMBO J, 19, 5288-5299.
PDB codes: 1f5m 1fl4
11080624 Z.Marković-Housley, G.Miglierini, L.Soldatova, P.J.Rizkallah, U.Müller, and T.Schirmer (2000).
Crystal structure of hyaluronidase, a major allergen of bee venom.
  Structure, 8, 1025-1035.
PDB codes: 1fcq 1fcu 1fcv
10523792 D.Volkmann, and F.Baluska (1999).
Actin cytoskeleton in plants: from transport networks to signaling networks.
  Microsc Res Tech, 47, 135-154.  
9891000 J.Rouvinen, J.Rautiainen, T.Virtanen, T.Zeiler, J.Kauppinen, A.Taivainen, and R.Mäntyjärvi (1999).
Probing the molecular basis of allergy. three-dimensional structure of the bovine lipocalin allergen Bos d 2.
  J Biol Chem, 274, 2337-2343.
PDB code: 1bj7
9990286 M.Van Troys, J.Vandekerckhove, and C.Ampe (1999).
Structural modules in actin-binding proteins: towards a new classification.
  Biochim Biophys Acta, 1448, 323-348.  
10467147 S.De Marino, M.A.Morelli, F.Fraternali, E.Tamborini, G.Musco, S.Vrtala, C.Dolecek, P.Arosio, R.Valenta, and A.Pastore (1999).
An immunoglobulin-like fold in a major plant allergen: the solution structure of Phl p 2 from timothy grass pollen.
  Structure, 7, 943-952.
PDB code: 1bmw
9649308 E.Korenbaum, P.Nordberg, C.Björkegren-Sjögren, C.E.Schutt, U.Lindberg, and R.Karlsson (1998).
The role of profilin in actin polymerization and nucleotide exchange.
  Biochemistry, 37, 9274-9283.  
9698363 J.C.Eads, N.M.Mahoney, S.Vorobiev, A.R.Bresnick, K.K.Wen, P.A.Rubenstein, B.K.Haarer, and S.C.Almo (1998).
Structure determination and characterization of Saccharomyces cerevisiae profilin.
  Biochemistry, 37, 11171-11181.
PDB code: 1ypr
9761827 N.M.Mahoney, and S.C.Almo (1998).
Crystallization and preliminary X-ray analysis of human platelet profilin complexed with an oligo proline peptide.
  Acta Crystallogr D Biol Crystallogr, 54, 108-110.  
9689336 R.Valenta, S.Vrtala, S.Laffer, S.Spitzauer, and D.Kraft (1998).
Recombinant allergens.
  Allergy, 53, 552-561.  
9417088 S.Ichikawa, H.Hatanaka, T.Yuuki, N.Iwamoto, S.Kojima, C.Nishiyama, K.Ogura, Y.Okumura, and F.Inagaki (1998).
Solution structure of Der f 2, the major mite allergen for atopic diseases.
  J Biol Chem, 273, 356-360.
PDB codes: 1ahk 1ahm
9484592 Y.A.Puius, N.M.Mahoney, and S.C.Almo (1998).
The modular structure of actin-regulatory proteins.
  Curr Opin Cell Biol, 10, 23-34.  
9345628 K.Moffat, and Z.Ren (1997).
Synchrotron radiation applications to macromolecular crystallography.
  Curr Opin Struct Biol, 7, 689-696.  
9409807 K.Schlüter, B.M.Jockusch, and M.Rothkegel (1997).
Profilins as regulators of actin dynamics.
  Biochim Biophys Acta, 1359, 97.  
9407048 M.Van Troys, D.Dewitte, J.L.Verschelde, M.Goethals, J.Vandekerckhove, and C.Ampe (1997).
Analogous F-actin binding by cofilin and gelsolin segment 2 substantiates their structural relationship.
  J Biol Chem, 272, 32750-32758.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.