Insecticidal delta-endotoxin Cyt2Ba from Bacillus thuringiensis: Difference between revisions

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Eran Hodis, Alexander Berchansky, Joel L. Sussman, Eric Martz, Jaime Prilusky, Michal Harel, David Canner

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 Cyt2Ba shares only 16% sequence identity to VVA2 ([[1pp0]]), nevertheless they both adopt a cytolysin fold and their structure is very similar (see their <scene name='Cyt2Ba/Cyt2ba_vva/2'>structural alignment</scene>).
-A striking similarity is observed between the structures of the endogenously cleaved Cyt2Ba <scene name='Cyt2Ba/Cyt2ba_monomer/1'>monomer</scene> (gray) and the <scene name='Cyt2Ba/Alignment/1'>corresponding region</scene> within the inactive protoxin  <scene name='Cyt2Ba/Dimer/1'>dimer</scene> of Cyt2Aa (monomers A and B of Cyt2Aa shown red and blue, respectively, the N- and C-termini are shown in spacefill representation). Each monomer of Cyt2Aa ([[1cby]]), consists of an extra β-strand at its N-terminus and α-helix at its C-terminus compared to the cleaved Cyt2Ba. The  <scene name='Cyt2Ba/Dimer_mesh/7'>dimer interface</scene> of Cyt2Aa is held together by the intertwined N-terminal strands from both monomers. The cleavage of Cyt2Aa <scene name='Cyt2Ba/Dimer_mesh/9'>removes</scene> the N and C termini segments, thereby preventing dimer formation and hence releasing a <scene name='Cyt2Ba/Monomer_toxin/2'>monomer active toxin</scene>. Similarly, it was shown that in Cyt2Ba the proteolysis causes the removal of 34 amino acids at its N-terminal and 28 or 30 residues at its C-terminus forming the crystallized toxic monomer.
+A striking similarity is observed between the structures of the endogenously cleaved Cyt2Ba <scene name='Cyt2Ba/Cyt2ba_monomer/1'>monomer</scene> (gray) and the <scene name='Cyt2Ba/Alignment/1'>corresponding region</scene> within the inactive protoxin  <scene name='Cyt2Ba/Dimer/1'>dimer</scene> of Cyt2Aa (monomers A and B of Cyt2Aa shown red and blue, respectively, the N- and C-termini are shown in spacefill representation). Each monomer of Cyt2Aa ([[1cby]]), consists of an extra β-strand at its N-terminus and α-helix at its C-terminus compared to the cleaved Cyt2Ba. The  <scene name='Cyt2Ba/Dimer_mesh/7'>dimer interface</scene> of Cyt2Aa is held together by the intertwined N-terminal strands from both monomers. The cleavage of Cyt2Aa <scene name='Cyt2Ba/Dimer_mesh/9'>removes</scene> the N and C termini segments, thereby preventing dimer formation and hence releasing a <scene name='Cyt2Ba/Monomer_toxin/3'>monomer active toxin</scene>. Similarly, it was shown that in Cyt2Ba the proteolysis causes the removal of 34 amino acids at its N-terminal and 28 or 30 residues at its C-terminus forming the crystallized toxic monomer.
 ===Conclusions===