PDBsum entry 1kfp

Antibiotic

PDB id: 1kfp

Contents

Protein chain

19 a.a.

PDB id:

1kfp

Name:

Antibiotic

Title:

Solution structure of the antimicrobial 18-residue gomesin

Structure:

Gomesin. Chain: a. Engineered: yes

Source:

Synthetic: yes. Acanthoscurria gomesiana. Mygalomorphae spider. Organism_taxid: 115339

NMR struc:

20 models

Authors:

N.Mandard,P.Bulet,A.Caille,S.Daffre,F.Vovelle

Key ref:

N.Mandard et al. (2002). The solution structure of gomesin, an antimicrobial cysteine-rich peptide from the spider. Eur J Biochem, 269, 1190-1198. PubMed id: 11856345 DOI: 10.1046/j.0014-2956.2002.02760.x

Date:

22-Nov-01 Release date: 10-Apr-02

Protein chain

P82358  (GOME_ACAGO) -  Gomesin from Acanthoscurria gomesiana

Seq: 84 a.a.

Struc: 19 a.a.*

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

DOI no: 10.1046/j.0014-2956.2002.02760.x

Eur J Biochem 269:1190-1198 (2002)

PubMed id: 11856345

The solution structure of gomesin, an antimicrobial cysteine-rich peptide from the spider.

N.Mandard, P.Bulet, A.Caille, S.Daffre, F.Vovelle.

ABSTRACT

Gomesin is the first peptide isolated from spider exhibiting antimicrobial activities. This highly cationic peptide is composed of 18 amino-acid residues including four cysteines forming two disulfide linkages. The solution structure of gomesin has been determined using proton two-dimensional NMR (2D-NMR) and restrained molecular dynamics calculations. The global fold of gomesin consists in a well-resolved two-stranded antiparallel betasheet connected by a noncanonical betaturn. A comparison between the structures of gomesin and protegrin-1 from porcine and androctonin from scorpion outlines several common features in the distribution of hydrophobic and hydrophilic residues. The N- and C-termini, the betaturn and one face of the betasheet are hydrophilic, but the hydrophobicity of the other face depends on the peptide. The similarities suggest that the molecules interact with membranes in an analogous manner. The importance of the intramolecular disulfide bridges in the biological activity of gomesin is being investigated.

Selected figure(s)

Figure 4.
Fig. 4. Representations of the polypeptide backbone of gomesin and of the central hydrophobic cluster. (A) stereoview of a superposition of the backbones of the 20 final structures. The structures are best fitted on the N-C -C' atoms of the well-defined sheet. (B) schematic representation of the overall fold with the strands represented as arrows.

Figure 5.
Fig. 5. Distribution of hydrophobic potentials. Middle and right: orthographic view of the hydrophobic potentials at the connolly surfaces (radius 1.4 Å) of gomesin (top), protegrin (middle) and androctonin (bottom). Left: schematic representations of the peptide backbones indicating the orientation in the left orthographic view pictures. Hydrophobicity increases from blue to brown while green is a colour halfway for intermediate potentials.

The above figures are reprinted by permission from the Federation of European Biochemical Societies: Eur J Biochem (2002, 269, 1190-1198) copyright 2002.

Figures were selected by the author.