PDBsum entry 5e5q

Antimicrobial protein

PDB id: 5e5q

Contents

Protein chains

63 a.a.

Waters ×154

PDB id:

5e5q

Name:

Antimicrobial protein

Title:

Racemic snakin-1 in p21/c

Structure:

Snakin-1. Chain: a, b. Fragment: unp residues 26-88. Engineered: yes

Source:

Synthetic: yes. Solanum tuberosum. Potato. Organism_taxid: 4113

Resolution:

1.60Å R-factor: 0.238 R-free: 0.283

Authors:

H.Yeung,C.J.Squire,Y.Yosaatmadja,S.Panjikar,E.N.Baker,P.W.R.Harris, M.A.Brimble

Key ref:

H.Yeung et al. (2016). Radiation Damage and Racemic Protein Crystallography Reveal the Unique Structure of the GASA/Snakin Protein Superfamily. Angew Chem Int Ed Engl, 55, 7930-7933. PubMed id: 27145301 DOI: 10.1002/anie.201602719

Date:

09-Oct-15 Release date: 18-May-16

Protein chains

Q948Z4  (SNAK1_SOLTU) -  Snakin-1 from Solanum tuberosum

Seq: 88 a.a.

Struc: 63 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

DOI no: 10.1002/anie.201602719

Angew Chem Int Ed Engl 55:7930-7933 (2016)

PubMed id: 27145301

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

H.Yeung, C.J.Squire, Y.Yosaatmadja, S.Panjikar, G.López, A.Molina, E.N.Baker, P.W.Harris, M.A.Brimble.

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.