Structural highlights
Publication Abstract from PubMed
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 A 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.
Radiation Damage and Racemic Protein Crystallography Reveal the Unique Structure of the GASA/Snakin Protein Superfamily.,Yeung H, Squire CJ, Yosaatmadja Y, Panjikar S, Lopez G, Molina A, Baker EN, Harris PW, Brimble MA Angew Chem Int Ed Engl. 2016 May 4. doi: 10.1002/anie.201602719. PMID:27145301[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Yeung H, Squire CJ, Yosaatmadja Y, Panjikar S, Lopez G, Molina A, Baker EN, Harris PW, Brimble MA. Radiation Damage and Racemic Protein Crystallography Reveal the Unique Structure of the GASA/Snakin Protein Superfamily. Angew Chem Int Ed Engl. 2016 May 4. doi: 10.1002/anie.201602719. PMID:27145301 doi:http://dx.doi.org/10.1002/anie.201602719
