PDBsum entry 1e16

Hydrolase

PDB id: 1e16

Contents

Protein chain

454 a.a.

Theoretical model

PDB id:

1e16

Name:

Hydrolase

Title:

Beta subunit of mitochondrial f1-atpase from sorghum line cs3541 fertility restorer of a1-male sterile cytoplasm

Structure:

F1-atp synthase, beta subunit. Chain: a. Synonym: atpb, atp2, atpb ec: 3.6.1.34

Source:

Sorghum bicolor. Sorghum. Atcc: cs3541. Tissue: coleoptile. Organelle: mitochondria. Cellular_location: mitochondria. Gene: atpb. Strain: cv. Cs3541. Other_details: the seuquence was deduced from the cdna and

Authors:

P.Jaiswal

Key ref:

P.Neudecker et al. (2001). Allergic cross-reactivity made visible: solution structure of the major cherry allergen Pru av 1. J Biol Chem, 276, 22756-22763. PubMed id: 11287426 DOI: 10.1074/jbc.M101657200

Date:

23-Apr-00 Release date: 23-May-00

Protein chain

O24346  (O24346_SORBI) -  ATP synthase subunit beta (Fragment)

Seq: 454 a.a.

Struc: 454 a.a.

DOI no: 10.1074/jbc.M101657200

J Biol Chem 276:22756-22763 (2001)

PubMed id: 11287426

Allergic cross-reactivity made visible: solution structure of the major cherry allergen Pru av 1.

P.Neudecker, K.Schweimer, J.Nerkamp, S.Scheurer, S.Vieths, H.Sticht, P.Rösch.

ABSTRACT

Birch pollinosis is often accompanied by hypersensitivity to fruit as a consequence of the cross-reaction of pollen allergen-specific IgE antibodies with homologous food proteins. To provide a basis for examining the cross-reactivity on a structural level, we used heteronuclear multidimensional NMR spectroscopy to determine the high-resolution three-dimensional structure of the major cherry allergen, Pru av 1, in solution. Based on a detailed comparison of the virtually identical structures of Pru av 1 and Bet v 1, the major birch pollen allergen, we propose an explanation for a significant aspect of the observed cross-reactivity pattern among the family of allergens under consideration. The large hydrophobic cavity expected to be important for the still unknown physiological function of Bet v 1 is conserved in Pru av 1. Structural homology to a domain of human MLN64 associated with cholesterol transport suggests phytosteroids as putative ligands for Pru av 1. NMR spectroscopy provides experimental evidence that Pru av 1 interacts with phytosteroids, and molecular modeling shows that the hydrophobic cavity is large enough to accommodate two such molecules.

Selected figure(s)

Figure 5.
Fig. 5. Backbone overlay of the lowest energy solution structure of Pru av 1 (green) and the crystal structure of Bet v 1 (orange) in complex with one (top) and two (bottom) castasterone molecules (representative models). The same view is shown as in Figs. 3 and 4. The loop from Glu60 to Tyr64 is indicated by an arrow. The overlay was performed using Sybyl 6.5 (Tripos Inc.).

Figure 9.
Fig. 9. Backbone overlay of the lowest energy solution structure of Pru av 1 (green) and the crystal structure of the START domain of MLN64 (red). The same view is shown as in Figs. 3-5. The overlay was performed using Sybyl 6.5 (Tripos Inc.).

The above figures are reprinted by permission from the ASBMB: J Biol Chem (2001, 276, 22756-22763) copyright 2001.

Figures were selected by an automated process.