PDBsum entry 1plm

Complex (protein/peptide)

PDB id: 1plm

Contents

Protein chain

130 a.a.

Ligands

PRO-PRO-PRO-PRO-PRO-PRO-PRO-PRO

Theoretical model

PDB id:

1plm

Name:

Complex (protein/peptide)

Title:

Arabidopsis profilin 1 complexed with poly-l-proline, theoretical model

Structure:

Profilin 1. Chain: a. Engineered: yes. Poly-l-proline. Chain: b. Engineered: yes

Source:

Arabidopsis thaliana. Mouse-ear cress. Expressed in: escherichia coli. Synthetic: non-biological source

Authors:

R.T.Shigeta,K.S.Thorn,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

Date:

09-Jan-98 Release date: 29-Apr-98

Protein chain

Q42449  (PROF1_ARATH) -  Profilin-1

Seq: 131 a.a.

Struc: 130 a.a.

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.

ABSTRACT

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.