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

Revision as of 14:53, 25 May 2008 view source Alexander Berchansky (talk \| contribs) 29,637 edits No edit summary ← Older edit		Revision as of 14:53, 25 May 2008 view source Alexander Berchansky (talk \| contribs) 29,637 edits No edit summary Newer edit →
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	The crystal structure of the proteolytically activated, monomeric form of Cyt2Ba was solved to 1.8Å resolution. It is composed of a single domain of <scene name='Cyt2Ba/Alpha_beta/2'>α/β</scene> architecture with a <scene name='Cyt2Ba/Beta/1'>β-sheet</scene> surrounded by two <scene name='Cyt2Ba/Alpha/1'>α-helical</scene> layers representing a cytolysin fold. The sheet consists of six anti-parallel β-strands (β1-β6) flanked by an α-helix layer composed of α1, α2 on one side, and by a second α-helix layer composed of α3-α5 on the other. The four longest β-strands (β2-β5) of the central β-sheet have a modified Greek-key topology.		The crystal structure of the proteolytically activated, monomeric form of Cyt2Ba was solved to 1.8Å resolution. It is composed of a single domain of <scene name='Cyt2Ba/Alpha_beta/2'>α/β</scene> architecture with a <scene name='Cyt2Ba/Beta/1'>β-sheet</scene> surrounded by two <scene name='Cyt2Ba/Alpha/1'>α-helical</scene> layers representing a cytolysin fold. The sheet consists of six anti-parallel β-strands (β1-β6) flanked by an α-helix layer composed of α1, α2 on one side, and by a second α-helix layer composed of α3-α5 on the other. The four longest β-strands (β2-β5) of the central β-sheet have a modified Greek-key topology.