In Silico Modeling and Functional Interpretations of Cry1Ab15 Toxin from Bacillus thuringiensis BtB-Hm-16.
The theoretical homology based structural model of Cry1Ab15 δ-endotoxin produced by Bacillus thuringiensis BtB-Hm-16 was predicted using the Cry1Aa template (resolution 2.25?Å). The Cry1Ab15 resembles the template structure by sharing a common three-domain extending conformation structure responsibl...
| Publicado en: | BioMed Research International Vol. 2013; pp. 471636 - 471637 |
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| Autor principal: | |
| Formato: | Journal Article |
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Wiley-Blackwell
2013
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| Acceso en línea: | Ver este registro en EBSCOhost |
| fields | @attributes: recordID: 1 pdfLink: plink: https://search.ebscohost.com/login.aspx?direct=true&db=ccm&AN=104114361&site=ehost-live header: @attributes: shortDbName: ccm uiTerm: 104114361 longDbName: CINAHL Complete uiTag: AN controlInfo: bkinfo: dissinfo: jinfo: jid: 23146133 FT2T jtl: BioMed Research International issn: 23146133 maglogo: N pubinfo: dt: 2013 vid: 2013 pid: 480 pub: Wiley-Blackwell place: Malden, Massachusetts artinfo: ui: 104114361 2012372187 NLM24228249 PMC3818814 104114361 ppf: 471636 ppct: 1 formats: fmt: @attributes: type: P tig: atl: In Silico Modeling and Functional Interpretations of Cry1Ab15 Toxin from Bacillus thuringiensis BtB-Hm-16. aug: au: Kashyap, Sudhanshu affil: National Bureau of Agriculturally Important Microorganisms (ICAR), Kusmaur, Kaithauli, Maunath Bhanjan, Uttar Pradesh 275101, India. sug: subj: Bacterial Proteins Endotoxins Proteins Molecular Structure Amino Acids Bacillus Computer Simulation Genetic Techniques ab: The theoretical homology based structural model of Cry1Ab15 δ-endotoxin produced by Bacillus thuringiensis BtB-Hm-16 was predicted using the Cry1Aa template (resolution 2.25?Å). The Cry1Ab15 resembles the template structure by sharing a common three-domain extending conformation structure responsible for pore-forming and specificity determination. The novel structural differences found are the presence of ß0 and a3, and the absence of a7b, ß1a, a10a, a10b, ß12, and a11a while a9 is located spatially downstream. Validation by SUPERPOSE and with the use of PROCHECK program showed folding of 98% of modeled residues in a favourable and stable orientation with a total energy Z-score of -6.56; the constructed model has an RMSD of only 1.15?Å. These increments of 3D structure information will be helpful in the design of domain swapping experiments aimed at improving toxicity and will help in elucidating the common mechanism of toxin action. pubtype: Academic Journal doctype: Journal Article ougenre: Article language: English refInfo: holdings: @attributes: islocal: N |
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