Backbone and side chain chemical shift assignments of apolipophorin III from Galleria mellonella.
Apolipophorin III, a 163 residue monomeric protein from the greater wax moth Galleria mellonella (abbreviated as apoLp-IIIGM), has roles in upregulating expression of antimicrobial proteins as well as binding and deforming bacterial membranes. Due to its similarity to vertebrate apolipoproteins there is interest in performing atomic resolution analysis of apoLp-IIIGM as part of an effort to better understand its mechanism of action in innate immunity. In the first step towards structural characterization of apoLp-IIIGM, 99 % of backbone and 88 % of side chain (1)H, (13)C and (15)N chemical shifts were assigned. TALOS+ analysis of the backbone resonances has predicted that the protein is composed of five long helices, which is consistent with the reported structures of apolipophorins from other insect species. The next stage in the characterization of apoLp-III from G. mellonella will be to utilize these resonance assignments in solving the solution structure of this protein.
Department of Chemistry and Biochemistry, California State University Northridge, 18111 Nordhoff St., Northridge, CA, 91330-8262, USA. karin.crowhurst@csun.edu.
Karin A
KA
Crowhurst
Department of Chemistry and Biochemistry, California State University Long Beach, 1250 Bellflower Blvd., Long Beach, CA, 90840-9507, USA.
James V C
JV
Horn
Department of Chemistry and Biochemistry, California State University Long Beach, 1250 Bellflower Blvd., Long Beach, CA, 90840-9507, USA.
Paul M M
PM
Weers
D000818:Animals; D001053:Apolipoproteins / Q000737:chemistry*; D019476:Insect Proteins / Q000737:chemistry*; D009036:Moths; D019906:Nuclear Magnetic Resonance, Biomolecular
D001053:Apolipoproteins; D019476:Insect Proteins; C042470:apolipophorin III
Apolipophorin III; Chemical shift assignment; Exchangeable apolipoprotein; Galleria mellonella; NMR; apoLp-III