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Line 19: |
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| The Cys429 involved in the disulfide bond between the HC and the LC can't be shown here due to the condition for getting the crystal structure. | | The Cys429 involved in the disulfide bond between the HC and the LC can't be shown here due to the condition for getting the crystal structure. |
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| *The light chain of Clostridium botulinum neurotoxin serotype A has 11 α-helices :
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| **Helix 1 : <scene name='60/604485/H1/2'>H1</scene>
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| **Helix 2 : <scene name='60/604485/H2/1'>H2</scene> (we can notice the kink formed by <scene name='60/604485/Thr101/1'>Thr101</scene>, who may interact with an H from the N of Gly104)
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| **Helix 4 : <scene name='60/604485/H4/1'>H4</scene>
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| **Helix 5 : <scene name='60/604485/H5/1'>H5</scene>
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| **Helix 6 : <scene name='60/604485/H6/1'>H6</scene>
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| **Helix 7 : <scene name='60/604485/H7/1'>H7</scene>
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| **Helix 8 : <scene name='60/604485/H8/1'>H8</scene>
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| **Helix 9 : <scene name='60/604485/H9/1'>H9</scene>
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| **Helix 10 : <scene name='60/604485/H10/1'>H10</scene>
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| **Helix 11 : <scene name='60/604485/H11/1'>H11</scene>
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| **Helix 12 : <scene name='60/604485/H12/1'>H12</scene>
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| * It also has three 3-10 helices :
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| **Helix 3 : <scene name='60/604485/H3/2'>H3</scene>
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| **Helix 13 : <scene name='60/604485/H13/1'>H13</scene>
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| **Helix 14 : <scene name='60/604485/H14/1'>H14</scene>
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| * There are several <scene name='60/604485/Sheets/1'>β sheets </scene> that are anti parallel except <scene name='60/604485/Sheets_parrallel/1'>this one.</scene>
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| * An interesting structure is also a typical <scene name='60/604485/Betaturn/1'>β-turn</scene> : indeed the chain makes a sharp reversal by 180° within 4 residues, moreover Cα from the ''i'' residue and the Cα from the ''i+3'' residue are separated by less than 7 angstroms.
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| The Cys429 involved in the disulfide bond between the HC and the LC can't be shown here due to the condition for getting the crystal structure.
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| === Mechanism === | | === Mechanism === |