User:Mitchell Long/Sandbox 1: Difference between revisions
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<p>'''Structure homology'''-There is a great deal of sequence homology and structural coservation between the α and β subunits. When superimposed over the barrels of the alpha and beta subunits with a deviation of 0.62Å for 42 equivalent α carbons. The region of the beta subunit that contains the 29 residue deletion with respect to the alpha subunit differs notably in arrangement<ref name=Fisher, A.J.>PMID: 7756289</ref> . In the alpha subunit, the α7a helix is straight and extends toward the beta subunit. The region involved with dimerization, helices α and β are exceptionally similar in superposition. | <p>'''Structure homology'''-There is a great deal of sequence homology and structural coservation between the α and β subunits. When superimposed over the barrels of the alpha and beta subunits with a deviation of 0.62Å for 42 equivalent α carbons. The region of the beta subunit that contains the 29 residue deletion with respect to the alpha subunit differs notably in arrangement<ref name=Fisher, A.J.>PMID: 7756289</ref> . In the alpha subunit, the α7a helix is straight and extends toward the beta subunit. The region involved with dimerization, helices α and β are exceptionally similar in superposition. | ||
</p> | </p> | ||
<p>'''Active Site and Alpha Subunit'''-the <scene name='User:Mitchell_Long/Sandbox_1/Yellow_sheets/1'>flavin binding pocket</scene> of bacterial luciferase is a large open cavity that is accessible to solvent via an opening located at the C-terminal ends of the ǰ | <p>'''Active Site and Alpha Subunit'''-the <scene name='User:Mitchell_Long/Sandbox_1/Yellow_sheets/1'>flavin binding pocket</scene> of bacterial luciferase is a large open cavity that is accessible to solvent via an opening located at the C-terminal ends of the ǰ strands of the TIM-barrel structure<ref Campbell, Z.T.>PMID: 19435287</ref>. During the first step of the oxidation reaction, FMNH<sub>2</sub> binds to the flavin binding pocket and the enzyme undergoes a conformational change that blocks water in the surrounding environment from accessing both the excited peroxydihydroflavin intermediate. Next, O<sub>2</sub> and a long chain aldehyde bind to the FMNH<sub>2</sub> luciferase complex and a two step oxidatino reaction occurs. | ||
.</p> | .</p> | ||
<scene name='User:Mitchell_Long/Sandbox_1/Hetero_translucent/1'>Heterodimer</scene> | <scene name='User:Mitchell_Long/Sandbox_1/Hetero_translucent/1'>Heterodimer</scene> | ||
