Sandbox Reserved 951: Difference between revisions
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=====Interaction with ATP===== | =====Interaction with ATP===== | ||
[[Image:Luciferin_bounding_to_luciferase.jpg|300px|left|thumb|Hydrogen bonding between Luciferase and substrates luciferin (green), ATP (violet) and Mg2+]] | |||
We find a signal motif in luciferase which is <scene name='60/604470/Atp_binding_signal_motif/1'>[STG]-[STG]-G-[ST]-[ST]-[TSE]-[GS]-x-[PALIVM]-K</scene> where some residue like lysine are always conserved. This pattern enables ATP binding thanks to hydrogen bonds between residues and phosphates of ATP. There is another pattern : <scene name='60/604470/Adenosine_ring_binding/1'>[YFW]-[GASW]-x-[TSA]-E</scene> which takes a particular conformation because of hydrogen bonds between residues and maintain the adenosin ring of ATP. | We find a signal motif in luciferase which is <scene name='60/604470/Atp_binding_signal_motif/1'>[STG]-[STG]-G-[ST]-[ST]-[TSE]-[GS]-x-[PALIVM]-K</scene> where some residue like lysine are always conserved. This pattern enables ATP binding thanks to hydrogen bonds between residues and phosphates of ATP. There is another pattern : <scene name='60/604470/Adenosine_ring_binding/1'>[YFW]-[GASW]-x-[TSA]-E</scene> which takes a particular conformation because of hydrogen bonds between residues and maintain the adenosin ring of ATP. | ||
=====Interaction with luciferin===== | =====Interaction with luciferin===== | ||
Luciferase holds the luciferin with the specific residues <scene name='60/604470/Residues_helding_luciferin/1'>arginin 218, phenylalanin 247, serin 347 and adenin 348</scene>, still with hydrogen bounds. This bindings makes the carboxylate oxygen of luciferin points toward the α phosphate of ATP, so the oxygen is well-positionned to attack the α phosphate. This promotes the luciferin-AMP formation. | Luciferase holds the luciferin with the specific residues <scene name='60/604470/Residues_helding_luciferin/1'>arginin 218, phenylalanin 247, serin 347 and adenin 348</scene>, still with hydrogen bounds. This bindings makes the carboxylate oxygen of luciferin points toward the α phosphate of ATP, so the oxygen is well-positionned to attack the α phosphate. This promotes the luciferin-AMP formation. | ||
