PDBsum entry: 1aun

Antifungal protein

PDB id: 1aun

Contents

Protein chain

208 a.a. *

Waters ×89

* Residue conservation analysis

PDB id:

1aun

Name:

Antifungal protein

Title:

Pathogenesis-related protein 5d from nicotiana tabacum

Structure:

Pr-5d. Chain: a. Synonym: osmotin-like protein

Source:

Nicotiana tabacum. Common tobacco. Organism_taxid: 4097. Strain: samsun nn. Cell: cultured cell. Cellular_location: vacuole

Resolution:

1.80Å R-factor: 0.169 R-free: 0.219

Authors:

H.Koiwa,H.Kato,T.Nakatsu,J.Oda,Y.Yamada,F.Sato

Key ref:

H.Koiwa et al. (1999). Crystal structure of tobacco PR-5d protein at 1.8 A resolution reveals a conserved acidic cleft structure in antifungal thaumatin-like proteins. J Mol Biol, 286, 1137-1145. PubMed id: 10047487 DOI: 10.1006/jmbi.1998.2540

Date:

29-Aug-97 Release date: 04-Mar-98

Protein chain

P25871  (OLPA_TOBAC) -  Osmotin-like protein

Seq: 251 a.a.

Struc: 208 a.a.

 Gene Ontology (GO) functional annotation 

• Biological process: response to biotic stimulus (2 terms)

DOI no: 10.1006/jmbi.1998.2540

J Mol Biol 286:1137-1145 (1999)

PubMed id: 10047487

Crystal structure of tobacco PR-5d protein at 1.8 A resolution reveals a conserved acidic cleft structure in antifungal thaumatin-like proteins.

H.Koiwa, H.Kato, T.Nakatsu, J.Oda, Y.Yamada, F.Sato.

ABSTRACT

The crystal structure of tobacco PR-5d, an antifungal thaumatin-like protein isolated from cultured tobacco cells, was determined at the resolution of 1.8 A. The structure consists of 208 amino acid residues and 89 water molecules with a crystallographic R-factor of 0.169. The model has good stereochemistry, with respective root-mean-square deviations from the ideal values for bond and angle distances of 0.007 A and 1.542 degrees. Of the homologous PR-5 proteins, only those with antifungal activity had a common motif, a negatively charged surface cleft. This cleft is at the boundary between domains I and II, with a bottom part consisting of a three-stranded antiparallel beta-sheet in domain I. The acidic residues located in the hollow of the cleft form the beta-sheet region. Sequence and secondary structure analyses showed that the amino acid residues comprising the acidic cleft of PR-5d are conserved among other antifungal PR-5 proteins. This is the first report on the high-resolution crystal structure of an antifungal PR-5 protein. This structure provides insight into the function of pathogenesis-related proteins.

Selected figure(s)

Figure 4.
Figure 4. View of the surface topology of (a) PR-5d, (b) zeamatin and (c) thaumatin showing the solvent-accessible surface and surface electrostatic potential. The protein surface is colored according to the electrostatic potential, ranging from blue (most positive) to white (neutral) to red (most negative). The protein orientations (left to right) are similar to those shown in Figure 2 (top to bottom). The Figure was produced using (GRASP; [Nicholls and Honig 1991]).

Figure 6.
Figure 6. Hydrophobic residues (yellow) exposed to the solvent-accessible surfaces of (a) PR-5d, (b) zeamatin and (c) thaumatin. The orientations of the middle and right of the molecule are the same as the left and middle ones shown in Figure 4. The left molecules are tilted to show the characteristic phenylalanine residues (arrows) in the acidic cleft region.

The above figures are reprinted by permission from Elsevier: J Mol Biol (1999, 286, 1137-1145) copyright 1999.

Figures were selected by an automated process.