Sandbox Reserved 951: Difference between revisions
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The active site is not strictly highlighted according to the actual state of studies but some residues and motifs strongly modified have been determined and this conformation enables to find the active site. Many of these conserved residues are located on the core of the β-barrel, on the small C-terminal domain and in the surface of the N-terminal domain, which forms a <scene name='60/604470/Depression_c-ter_and_n-ter/1'>depression</scene>. However, this depression 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. This conformational change provides a suitable environment for light production because of exclusion of water molecules from the active site, favouring intramolecular reactions. Residues also follow a <scene name='60/604470/Cleft/1'>cleft</scene> caused by of the <scene name='60/604470/Beta_sheet_b/3'>Beta-sheet B</scene> against the <scene name='60/604470/Beta_barrel/3'>Beta-barrel</scene>.<ref name =''fourth'>PMID:8805533</ref> | The active site is not strictly highlighted according to the actual state of studies but some residues and motifs strongly modified have been determined and this conformation enables to find the active site. Many of these conserved residues are located on the core of the β-barrel, on the small C-terminal domain and in the surface of the N-terminal domain, which forms a <scene name='60/604470/Depression_c-ter_and_n-ter/1'>depression</scene>. However, this depression 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. This conformational change provides a suitable environment for light production because of exclusion of water molecules from the active site, favouring intramolecular reactions. Residues also follow a <scene name='60/604470/Cleft/1'>cleft</scene> caused by of the <scene name='60/604470/Beta_sheet_b/3'>Beta-sheet B</scene> against the <scene name='60/604470/Beta_barrel/3'>Beta-barrel</scene>.<ref name =''fourth'>PMID:8805533</ref> | ||
[[Image:Luciferin_bounding_to_luciferase.jpg|250px|right|thumb|Hydrogen bonding between Luciferase and substrates luciferin (green), ATP (violet) and Mg2+,<ref name='' | [[Image:Luciferin_bounding_to_luciferase.jpg|250px|right|thumb|Hydrogen bonding between Luciferase and substrates luciferin (green), ATP (violet) and Mg2+,<ref name=''''>[http://www.photobiology.info/ Photobiology]</ref>]] | ||
=====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>. Here some residues 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.<ref name =''fifth''>PMID:8805533</ref>, <ref name=''tenth''>[http://www.photobiology.info/ Photobiology]</ref> | 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>. Here some residues 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.<ref name =''fifth''>PMID:8805533</ref>, <ref name=''tenth''>[http://www.photobiology.info/ Photobiology]</ref> | ||
