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Radiation Damage and Racemic Protein Crystallography Reveal the Unique Structure of the GASA/Snakin Protein Superfamily.

Yeung H, Squire CJ, Yosaatmadja Y, Panjikar S, López G, Molina A, Baker EN, Harris PW, Brimble MA
Angew Chem Int Ed Engl 55 7930-3 (2016)
Related entries: 5e5q, 5e5y

Cited: 13 times
EuropePMC logo PMID: 27145301

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.

Articles - 5e5t mentioned but not cited (1)

  1. The missing link: covalent linkages in structural models. Nicholls RA, Wojdyr M, Joosten RP, Catapano L, Long F, Fischer M, Emsley P, Murshudov GN. Acta Crystallogr D Struct Biol 77 727-745 (2021)


Reviews citing this publication (5)

  1. Molecular and Biological Properties of Snakins: The Foremost Cysteine-Rich Plant Host Defense Peptides. Su T, Han M, Cao D, Xu M. J Fungi (Basel) 6 E220 (2020)
  2. An Overview of the Potentialities of Antimicrobial Peptides Derived from Natural Sources. Dini I, De Biasi MG, Mancusi A. Antibiotics (Basel) 11 1483 (2022)
  3. GASA Proteins: Review of Their Functions in Plant Environmental Stress Tolerance. Bouteraa MT, Ben Romdhane W, Baazaoui N, Alfaifi MY, Chouaibi Y, Ben Akacha B, Ben Hsouna A, Kačániová M, Ćavar Zeljković S, Garzoli S, Ben Saad R. Plants (Basel) 12 2045 (2023)
  4. Food Allergens of Plant Origin. Zhang Y, Che H, Li C, Jin T. Foods 12 2232 (2023)
  5. Novel protein science enabled by total chemical synthesis. Kent SBH. Protein Sci. 28 313-328 (2019)

Articles citing this publication (7)

  1. Influence of Cysteine and Tryptophan Substitution on DNA-Binding Activity on Maize α-Hairpinin Antimicrobial Peptide. Sousa DA, Porto WF, Silva MZ, da Silva TR, Franco OL. Molecules 21 (2016)
  2. Antimicrobial and structural insights of a new snakin-like peptide isolated from Peltophorum dubium (Fabaceae). Rodríguez-Decuadro S, Barraco-Vega M, Dans PD, Pandolfi V, Benko-Iseppon AM, Cecchetto G. Amino Acids 50 1245-1259 (2018)
  3. Enhanced expression of cysteine-rich antimicrobial peptide snakin-1 in Escherichia coli using an aggregation-prone protein coexpression system. Kuddus MR, Yamano M, Rumi F, Kikukawa T, Demura M, Aizawa T. Biotechnol. Prog. 33 1520-1528 (2017)
  4. The role of antimicrobial peptides in plant immunity. Campos ML, de Souza CM, de Oliveira KBS, Dias SC, Franco OL. J. Exp. Bot. 69 4997-5011 (2018)
  5. Gibberellin-regulated proteins: Emergent allergens. Iizuka T, Barre A, Rougé P, Charpin D, Scala E, Baudin B, Aizawa T, Sénéchal H, Poncet P. Front Allergy 3 877553 (2022)
  6. Mass Spectrometric Identification of Antimicrobial Peptides from Medicinal Seeds. Moyer TB, Brechbill AM, Hicks LM. Molecules 26 7304 (2021)
  7. The study on interacting factors and functions of GASA6 in Jatropha curcas L. Li X, Zhang MS, Zhao LQ, Ling-Hu QQ, Xu G. BMC Plant Biol 23 99 (2023)


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