Sandbox Reserved 1654: Difference between revisions
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<StructureSection load='2m13' size='340' side='left' caption='Caption for this structure' scene=''> | <StructureSection load='2m13' size='340' side='left' caption='Caption for this structure' scene=''> | ||
</StructureSection> | </StructureSection> | ||
About 54 residues with 6 cysteines and 2 histidines, conserved for all isoforms and species. The modification of one of the eight zinc ligands destabilize the connection to the mRNA. The domain includes : ***A Rubredoxin turn (Rd turn, residues 515-520), which is stabilized by hydrogen bonds between amide and sulfure. | About 54 residues with 6 cysteines and 2 histidines, conserved for all isoforms and species. The modification of one of the eight zinc ligands destabilize the connection to the mRNA. The domain includes : | ||
***A Rubredoxin turn (Rd turn, residues 515-520), which is stabilized by hydrogen bonds between amide and sulfure. | |||
***β-hairpin with β1 (residues 525-527) and β2 (residues 533-535) between which there is an helical turn stabilized by hydrogen bonds. | ***β-hairpin with β1 (residues 525-527) and β2 (residues 533-535) between which there is an helical turn stabilized by hydrogen bonds. | ||
***An α1 helix (residues 538-545) which forms the second bridge between the two zinc-binding sites. The surface-exposed face of the helix has a potential for specific intermolecular interactions with nucleic acids or proteins. | ***An α1 helix (residues 538-545) which forms the second bridge between the two zinc-binding sites. The surface-exposed face of the helix has a potential for specific intermolecular interactions with nucleic acids or proteins. | ||
