2L3I

Oxki4a, spider derived antimicrobial peptide

Summary for 2L3I

• Entry DOI: 10.2210/pdb2l3i/pdb
• NMR Information: BMRB: 17194
• Descriptor: AOXKI4A, antimicrobial peptide in spider venom (1 entity in total)
• Functional Keywords: antimicrobial peptide, antimicrobial protein
• Biological source: Oxyopes takobius (spider)
• Total number of polymer chains: 1
• Total formula weight: 3624.53

Authors

Vassilevski, A.A.,Dubovskii, P.V.,Samsonova, O.V.,Egorova, N.S.,Kozlov, S.A.,Feofanov, A.V.,Arseniev, A.S.,Grishin, E.V. (deposition date: 2010-09-14, release date: 2011-09-14, Last modification date: 2024-11-27)

Primary citation

Dubovskii, P.V.,Vassilevski, A.A.,Samsonova, O.V.,Egorova, N.S.,Kozlov, S.A.,Feofanov, A.V.,Arseniev, A.S.,Grishin, E.V.
Novel lynx spider toxin shares common molecular architecture with defense peptides from frog skin.
Febs J., 278:4382-4393, 2011

PubMed Abstract: A unique 30-residue cationic peptide oxyopinin 4a (Oxt 4a) was identified in the venom of the lynx spider Oxyopes takobius (Oxyopidae). Oxt 4a contains a single N-terminally located disulfide bond, Cys4-Cys10, and is structurally different from any spider toxin studied so far. According to NMR findings, the peptide is disordered in water, but assumes a peculiar torpedo-like structure in detergent micelles. It features a C-terminal amphipathic α-helical segment (body; residues 12-25) and an N-terminal disulfide-stabilized loop (head; residues 1-11), and has an unusually high density of positive charge in the head region. Synthetic Oxt 4a was produced and shown to possess strong and broad-spectrum cytolytic and antimicrobial activity. cDNA cloning showed that the peptide is synthesized in the form of a conventional prepropeptide with an acidic prosequence. Unlike other arachnid toxins, Oxt 4a exhibits striking similarity with defense peptides from the skin of ranid frogs that contain the so-called Rana-box motif (a C-terminal disulfide-enclosed loop). Parallelism or convergence is apparent on several levels: the structure, function and biosynthesis of a lynx spider toxin are mirrored by those of Rana-box peptides from frogs.

PubMed: 21933345
DOI: 10.1111/j.1742-4658.2011.08361.x

Experimental method

SOLUTION NMR