Two-dimensional1H NMR study of recombinant insect defensin A in water: Resonance assignments, secondary structure and global folding View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1992-05

AUTHORS

Jean-Marc Bonmatin, Jean-Luc Bonnat, Xavier Gallet, Françoise Vovelle, Marius Ptak, Jean-Marc Reichhart, Jules A. Hoffmann, Elisabeth Keppi, Michèle Legrain, Tilman Achstetter

ABSTRACT

A 500 MHz 2D 1H NMR study of recombinant insect defensin A is reported. This defense protein of 40 residues contains 3 disulfide bridges, is positively charged and exhibits antibacterial properties. 2D NMR maps of recombinant defensin A were fully assigned and secondary structure elements were localized. The set of NOE connectivities, 3JNH-alpha H coupling constants as well as 1H/2H exchange rates and delta delta/delta T temperature coefficients of NH protons strongly support the existence of an alpha-helix (residues 14-24) and of an antiparallel beta-sheet (residues 27-40). Models of the backbone folding were generated by using the DISMAN program and energy refined by using the AMBER program. This was done on the basis of: (i) 133 selected NOEs, (ii) 21 dihedral restraints from 3JNH-alpha H coupling constants, (iii) 12 hydrogen bonds mostly deduced from 1H/2H exchange rates or temperature coefficients, in addition to 9 initial disulfide bridge covalent constraints. The two secondary structure elements and the two bends connecting them involve approximately 70% of the total number of residues, which impose some stability in the C-terminal part of the molecule. The remaining N-terminal fragment forms a less well defined loop. This spatial organization, in which a beta-sheet is linked to an alpha-helix by two disulfide bridges and to a large loop by a third disulfide bridge, is rather similar to that found in scorpion charybdotoxin and seems to be partly present in several invertebrate toxins. More... »

PAGES

235-256

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf01875319

DOI

http://dx.doi.org/10.1007/bf01875319

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1006574569

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/1392568


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