Research Article
In Silico Modeling and Functional Interpretations of Cry1Ab15 Toxin from Bacillus thuringiensis BtB-Hm-16
Table 1
The comparison among three-domain structural components of Cry1Aa and Cry1Ab15 toxin molecules.
| Domain I | Domain II | Domain III | | Cry1Aa | Cry1Ab15 | | Cry1Aa | Cry1Ab15 | | Cry1Aa | Cry1Ab15 |
| β0 | — | Thr31-Tyr33 | α8a | Pro271-Glu274 | Pro271-Asn275 | α11a | Leu475-Lys477 | — | α1 | Pro35-Ser48 | Pro35-Ser48 | α8b | Ala284-Gln289 | Ser283-Ser290 | β13a | Ser486-Val488 | Ser487-Val489 | α2a | Aln54-Ile63 | Aln54-Trp65 | β2 | Asp298-His310 | Ile299-His310 | β13b | Ile498-Arg501 | Ile499-Arg502 | α2b | Pro70-Ile84 | Pro70-Ile84 | β3 | Phe313-Trp316 | Glu313-Ser324 | β14 | Gly505-Asn513 | Gly506-Asn514 | α3 | Glu90-Ala119 | Glu90-Ala119 | β4 | Gly318-Pro325 | Tyr359-Arg368 | β15 | Tyr522-Ser530 | Tyr523-Ala530 | α4 | Pro124-Leu148 | Pro124-Leu148 | α9 | Val326-Phe328 |
*
Ser409-Glu412 | β16 | Leu534-Ile540 | Leu534-Ile541 | α5 | Gln154-Trp182 | Val155-Trp182 | β5 | Val348-Ser351 | Leu380-Tyr390 | β17 | Arg543-Phe550 | Arg544-Phe551 | α6 | Ala186-Val218 | Ala186-Val218 | β6 | Ile357-Arg367 | Ala399-Tyr401 | α12a | Ser562-Ser564 | Ser563-Ser565 | α7a | Ser223-Thr239 | Ser223-Tyr250 | β7 | Leu380-Leu383 | Thr406-Asp408 | β18 | Arg566-Gly569 | Arg567-Phe571 | α7b | Leu241-Tyr250 | — | β8 | Gly385-Phe390 | His428-Arg437 | β19 | Ser580-His588 | Ser581-His589 | β1a | Glu266-Thr269 | — | β9 | Thr400-Tyr402 | Ile447-His457 | β20 | Val596-Pro605 | Val597-Pro606 | | | | α10a | Ser410-Asp412 | — | α13 | — | Phe611-Ala623 | | | | α10b | Pro423-Gly426 | — | | | | | | | β10 | His429-Val434 | Gln473-Pro475 | | | | | | | β11 | Phe452-His456 | Thr480-Leu482 | | | | | | | β12 | Thr471-Pro474 | — | | | |
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—: similar component not present. *Components in italics are spatially present at downstream sites.
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