Sandbox Reserved 951: Difference between revisions
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=====Interaction with ATP===== | =====Interaction with 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. | 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. | ||
[[Image:Luciferin_bounding_to_luciferase.jpg|300px|left|thumb|Hydrogen bonding between Luciferase and substrates luciferin (green), ATP (violet) and Mg2+]] | |||
=====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. | ||
=====Interaction with fatty acids===== | =====Interaction with fatty acids===== | ||
Fatty acids are highly similar to luciferin. Therefore, luciferase can use the luciferin binding site to bind fatty acids. That is why they can be used as substrates by luciferase and then, very high similar reaction as for luciferin occurs. | Fatty acids are highly similar to luciferin. Therefore, luciferase can use the luciferin binding site to bind fatty acids. That is why they can be used as substrates by luciferase and then, very high similar reaction as for luciferin occurs. | ||
