Sandbox Reserved 951: Difference between revisions
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However, this cleft is too large to enable interactions between residues and substrates, so it is thought that a conformational change occurs and sandwiches the substrates, forming the active site. | However, this cleft is too large to enable interactions between residues and substrates, so it is thought that a conformational change occurs and sandwiches the substrates, forming the active site. | ||
=====Interaction with ATP===== | =====Interaction with ATP===== | ||
We find a signal motif in luciferase which is [STG]-[STG]-G-[ST]-[ST]-[TSE]-[GS]-x-[PALIVM]-K where some residue like arginine are always conserved. This pattern enables ATP binding thanks to hydrogen bonds between residues and phosphates of ATP. There is another pattern : [YFW]-[GASW]-x-[TSA]-E 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 arginine are always conserved. This pattern enables ATP binding thanks to hydrogen bonds between residues and phosphates of ATP. There is another pattern : [YFW]-[GASW]-x-[TSA]-E 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 arginin 218, phenylalanin 247, serin 347 and adenin 348, 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 arginin 218, phenylalanin 247, serin 347 and adenin 348, 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. | ||
