1MMC

1H NMR STUDY OF THE SOLUTION STRUCTURE OF AC-AMP2

Summary for 1MMC

• Entry DOI: 10.2210/pdb1mmc/pdb
• NMR Information: BMRB: 6591,6637,6639,6647
• Descriptor: ANTIMICROBIAL PEPTIDE 2 (1 entity in total)
• Functional Keywords: antifungal antimicrobial, chitin-binding
• Biological source: Amaranthus caudatus (amaranth)
• Total number of polymer chains: 1
• Total formula weight: 3194.78

Authors

Martins, J.C.,Maes, D.,Loris, R.,Pepermans, H.A.M.,Wyns, L.,Willem, R.,Verheyden, P. (deposition date: 1995-10-25, release date: 1996-03-08, Last modification date: 2024-11-20)

Primary citation

Martins, J.C.,Maes, D.,Loris, R.,Pepermans, H.A.,Wyns, L.,Willem, R.,Verheyden, P.
H NMR study of the solution structure of Ac-AMP2, a sugar binding antimicrobial protein isolated from Amaranthus caudatus.
J.Mol.Biol., 258:322-333, 1996

PubMed Abstract: The conformation in water of antimicrobial protein 2 from Amaranthus caudatus (Ac-AMP2) was determined using 1H NMR, DIANA and restrained molecular modeling. Ac-AMP2 is a 30 amino acid residue, lectin-like protein that specifically binds to chitin, a polymer of beta-1,4-N-acetyl-D-glucosamine. After sequence specific resonance assignments, a total of 198 distance restraints were collected from 2D NOESY buildup spectra at 500 MHz at pH 2, supplemented by a 2D NOESY spectrum at 600 MHz. The location of the three previously unassigned disulfide bridges was determined from preliminary DIANA structures, using a statistical analysis of intercystinyl distances. The solution structure of Ac-AMP2 is presented as a set of 26 DIANA structures, further refined by restrained molecular dynamics using a simulated annealing protocol in the AMBER force field, with a backbone r.m.s.d. for the well defined Glu3-Cys28 segment of 0.69(+/-0.12) angstroms. The main structural element is an antiparallel beta-sheet from Met13 to Lys23 including a betaI-turn over Gln17-Phel8 with a beta bulge at Gly19. In addition, a beta'I turn over Arg6-Gly7, a beta'III turn over Ser11-Gly12 and a helical turn from Gly24 to Cys28 are identified. This structure is very similar to the equivalent regions of the X-ray structure of wheat germ agglutinin and the NMR structure of hevein.

PubMed: 8627629
DOI: 10.1006/jmbi.1996.0253

Experimental method

SOLUTION NMR