5E5T

Quasi-racemic snakin-1 in P1 after radiation damage

Summary for 5E5T

• Entry DOI: 10.2210/pdb5e5t/pdb
• Related: 5E5Q 5E5Y
• Descriptor: Snakin-1, D- snakin-1, FORMIC ACID, ... (5 entities in total)
• Functional Keywords: gasa/snakin, cysteine-rich antimicrobial peptide, antimicrobial protein
• Biological source: Solanum tuberosum (Potato); More
• Total number of polymer chains: 4
• Total formula weight: 28364.69

Authors

Yeung, H.,Squire, C.J.,Yosaatmadja, Y.,Panjikar, S.,Baker, E.N.,Harris, P.W.R.,Brimble, M.A. (deposition date: 2015-10-09, release date: 2016-05-18, Last modification date: 2025-04-02)

Primary citation

Yeung, H.,Squire, C.J.,Yosaatmadja, Y.,Panjikar, S.,Lopez, G.,Molina, A.,Baker, E.N.,Harris, P.W.,Brimble, M.A.
Radiation Damage and Racemic Protein Crystallography Reveal the Unique Structure of the GASA/Snakin Protein Superfamily.
Angew.Chem.Int.Ed.Engl., 55:7930-7933, 2016

PubMed Abstract: Proteins from the GASA/snakin superfamily are common in plant proteomes and have diverse functions, including hormonal crosstalk, development, and defense. One 63-residue member of this family, snakin-1, an antimicrobial protein from potatoes, has previously been chemically synthesized in a fully active form. Herein the 1.5 Å structure of snakin-1, determined by a novel combination of racemic protein crystallization and radiation-damage-induced phasing (RIP), is reported. Racemic crystals of snakin-1 and quasi-racemic crystals incorporating an unnatural 4-iodophenylalanine residue were prepared from chemically synthesized d- and l-proteins. Breakage of the C-I bonds in the quasi-racemic crystals facilitated structure determination by RIP. The crystal structure reveals a unique protein fold with six disulfide crosslinks, presenting a distinct electrostatic surface that may target the protein to microbial cell surfaces.

PubMed: 27145301
DOI: 10.1002/anie.201602719

Experimental method

X-RAY DIFFRACTION (1.572 Å)