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. Author manuscript; available in PMC: 2011 Aug 1.

Published in final edited form as: Biochim Biophys Acta. 2010 Mar 15;1800(8):824–833. doi: 10.1016/j.bbagen.2010.03.004

Fig. 1 — The signal sequences for both the HCH and LCH T. ni subunits are removed to maintain the same numerical assignments as cited in the original structural work [31]. * = identical residues; : = conserved residues; . = semi-conserved residues. The sequence alignments were performed using Clustal 2.0.11 multiple sequence alignment at http://www.ebi.ac.uk/Tools/clustalw2/index.html with known insect HCH and LCH sequences deposited at the National Center for Biotechnology Information (http://www.ncbi.nlm.nih.gov/). A. Sequence alignment for insect HCH subunits. C residues involved in inter- and intrasubunit disulside bonds are bolded and overlined; amino acid residues in ferroxidase center are italicized; amino acid residues engaged in the salt bridges and pi-cation interactions are shaded in grey. Sequences are from Manduca sexta (hawkmoth, Lepidoptera) [19], Calpodes ethlius (skipper butterfly, Lepidoptera) [21], Galleria mellonella (wax moth, Lepidoptera) [23], Nilaparvata lugens (plant hopper, Hemiptera) [22], Aedes aegypti (yellow fever mosquito, Diptera) [18], Drosophila melanogaster (fruit fly, Diptera) [20], Anopheles gambiae (malaria mosquito, Diptera) [80], Apriona germari (long horned beetle, Coleoptera) [24], Leptinotarsa decemlineata (Colorado potato beetle, Coleoptera [25], Glossina morsitans morsitans (tsetse fly, Diptera) [15], Bombus ignitus (bumble bee, Hymenoptera), [16, 17] and Trichoplusia ni (cabbage looper, Lepidoptera) [31]. B. Sequence alignment for insect LCH subunits. C residues and amino acid residues engaged in the salt bridges and pi-cation interactions are represented as described in (A). Putative N-glycosylation sites (N-X-S/T) are underlined. LCH subunit sequences are from the same species and references cited above; no LCH sequence was reported for B. ignitus.

Fig. 1 — The signal sequences for both the HCH and LCH T. ni subunits are removed to maintain the same numerical assignments as cited in the original structural work [31]. * = identical residues; : = conserved residues; . = semi-conserved residues. The sequence alignments were performed using Clustal 2.0.11 multiple sequence alignment at http://www.ebi.ac.uk/Tools/clustalw2/index.html with known insect HCH and LCH sequences deposited at the National Center for Biotechnology Information (http://www.ncbi.nlm.nih.gov/). A. Sequence alignment for insect HCH subunits. C residues involved in inter- and intrasubunit disulside bonds are bolded and overlined; amino acid residues in ferroxidase center are italicized; amino acid residues engaged in the salt bridges and pi-cation interactions are shaded in grey. Sequences are from Manduca sexta (hawkmoth, Lepidoptera) [19], Calpodes ethlius (skipper butterfly, Lepidoptera) [21], Galleria mellonella (wax moth, Lepidoptera) [23], Nilaparvata lugens (plant hopper, Hemiptera) [22], Aedes aegypti (yellow fever mosquito, Diptera) [18], Drosophila melanogaster (fruit fly, Diptera) [20], Anopheles gambiae (malaria mosquito, Diptera) [80], Apriona germari (long horned beetle, Coleoptera) [24], Leptinotarsa decemlineata (Colorado potato beetle, Coleoptera [25], Glossina morsitans morsitans (tsetse fly, Diptera) [15], Bombus ignitus (bumble bee, Hymenoptera), [16, 17] and Trichoplusia ni (cabbage looper, Lepidoptera) [31]. B. Sequence alignment for insect LCH subunits. C residues and amino acid residues engaged in the salt bridges and pi-cation interactions are represented as described in (A). Putative N-glycosylation sites (N-X-S/T) are underlined. LCH subunit sequences are from the same species and references cited above; no LCH sequence was reported for B. ignitus.