PDBsum entry 5cgo

Antimicrobial protein

PDB id: 5cgo

Contents

Protein chains

23 a.a.

23 a.a.

Waters ×45

PDB id:

5cgo

Name:

Antimicrobial protein

Title:

Structure of quasiracemic ala-magainin 2 with a beta amino acid substitution at position 13

Structure:

Acpc-13 derivative of ala-magainin 2. Chain: a, b. Engineered: yes. D-ala-magainin 2. Chain: c, d. Engineered: yes

Source:

Synthetic: yes. Synthetic construct. Organism_taxid: 32630. Organism_taxid: 32630

Resolution:

1.50Å R-factor: 0.175 R-free: 0.239

Authors:

Z.Hayouka,N.C.Thomas,D.E.Mortenson,K.A.Satyshur,B.Weisblum, K.T.Forest,S.H.Gellman

Key ref:

Z.Hayouka et al. (2015). Quasiracemate Crystal Structures of Magainin 2 Derivatives Support the Functional Significance of the Phenylalanine Zipper Motif. J Am Chem Soc, 137, 11884-11887. PubMed id: 26369301 DOI: 10.1021/jacs.5b07206

Date:

09-Jul-15 Release date: 23-Sep-15

Protein chains

P11006  (MAGA_XENLA) -  Magainins from Xenopus laevis

Seq: 303 a.a.

Struc: 23 a.a.*

Protein chains

No UniProt id for this chain

Struc: 23 a.a.

* PDB and UniProt seqs differ at 3 residue positions (black crosses)

DOI no: 10.1021/jacs.5b07206

J Am Chem Soc 137:11884-11887 (2015)

PubMed id: 26369301

Quasiracemate Crystal Structures of Magainin 2 Derivatives Support the Functional Significance of the Phenylalanine Zipper Motif.

Z.Hayouka, N.C.Thomas, D.E.Mortenson, K.A.Satyshur, B.Weisblum, K.T.Forest, S.H.Gellman.

ABSTRACT

Quasiracemic crystallography has been used to explore the significance of homochiral and heterochiral associations in a set of host-defense peptide derivatives. The previously reported racemic crystal structure of a magainin 2 derivative displayed a homochiral antiparallel dimer association featuring a "phenylalanine zipper" notable for the dual roles of phenylalanines in mediating dimerization and formation of an exposed hydrophobic swath. This motif is seen as well in two new quasiracemate crystals that contain the d form of the magainin 2 derivative along with an l-peptide in which one Ala has been replaced by a β-amino acid residue. This structural trend supports the hypothesis that the Phe zipper motif has functional significance.