Sandbox 167: Difference between revisions

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	Note the position of the tri-helix in front of the β-barrel opening, blocking substrate entry. Under a pH of 8, the protonation states of the four histidines are thought to drive a conformational change that opens and expands the β-barrel. Interestingly, the four histidines(H899, H909, H924 and H930) are conserved in another dinoflagellate, ''Pyrocystis ~~Lunula~~''. <ref name="papertwo">PMID:11747464</ref>		Note the position of the tri-helix in front of the β-barrel opening, blocking substrate entry. Under a pH of 8, the protonation states of the four histidines are thought to drive a conformational change that opens and expands the β-barrel. Interestingly, the four histidines(H899, H909, H924 and H930) are conserved in another dinoflagellate, ''Pyrocystis lunula''<ref name="papertwo">PMID:11747464</ref>. This seems to suggest a pH-dependant luciferase contol mechanism similiar to the proposed mechanism in ''L. polyedrum''. While related at the primary structure level, the structure of ''P. lunula'' luciferase has yet to be solved, so further structural similarities cannot be easily resolved.



	== Luciferase Reaction ==		== Luciferase Reaction ==