5CGO
Structure of quasiracemic Ala-Magainin 2 with a beta amino acid substitution at position 13
Summary for 5CGO
| Entry DOI | 10.2210/pdb5cgo/pdb |
| Related | 4MGP 5CGN |
| Descriptor | ACPC-13 derivative of Ala-Magainin 2, D-Ala-Magainin 2 (3 entities in total) |
| Functional Keywords | antimicrobial, quasiracemate, homochiral dimerization, beta amino acids, antimicrobial protein |
| Biological source | synthetic construct More |
| Total number of polymer chains | 4 |
| Total formula weight | 10036.08 |
| Authors | Hayouka, Z.,Thomas, N.C.,Mortenson, D.E.,Satyshur, K.A.,Weisblum, B.,Forest, K.T.,Gellman, S.H. (deposition date: 2015-07-09, release date: 2015-09-23, Last modification date: 2023-11-15) |
| Primary citation | Hayouka, Z.,Thomas, N.C.,Mortenson, D.E.,Satyshur, K.A.,Weisblum, B.,Forest, K.T.,Gellman, S.H. Quasiracemate Crystal Structures of Magainin 2 Derivatives Support the Functional Significance of the Phenylalanine Zipper Motif. J.Am.Chem.Soc., 137:11884-11887, 2015 Cited by PubMed 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crystals that contain the d form of the magainin 2 derivative along with an l-peptide in which one Ala has been replaced by a β-amino acid residue.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. PubMed: 26369301DOI: 10.1021/jacs.5b07206 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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