1mmc
From Proteopedia
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1H NMR STUDY OF THE SOLUTION STRUCTURE OF AC-AMP2
Overview
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.
About this Structure
1MMC is a Single protein structure of sequence from Amaranthus caudatus. Full crystallographic information is available from OCA.
Reference
H NMR study of the solution structure of Ac-AMP2, a sugar binding antimicrobial protein isolated from Amaranthus caudatus., Martins JC, Maes D, Loris R, Pepermans HA, Wyns L, Willem R, Verheyden P, J Mol Biol. 1996 May 3;258(2):322-33. PMID:8627629
Page seeded by OCA on Tue Nov 20 21:31:40 2007
