User:Mark Macbeth/Sandbox8: Difference between revisions
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The beta hairpin stabilizes the <scene name='81/811707/Beta_hairpin_stabilizing_tyrs/1'>conformation of Tyr335 and Tyr337</scene>, while also shaping one side of the channel which the peptide binds to.<ref name="Xiao" /> The <scene name='81/811707/Peptide_binding_site/1'>peptide binding groove</scene> is composed of residues 255-268.<ref name="Xiao" /> Lysine would have trouble coming down into the active site in its charged form, but it is facilitated by the faces of the flanking tyrosines.<ref name="Xiao" /> The orientation of the lysine is such that the amine-methyl bond is aligned towards the sulfur on SAM so that it can provide the methyl. There is an important water in the active site (Figure 2) as well that acts as a stabilizer for lysine, and helps to shift the lone pair on the nitrogen towards the sulfur of SAM. <ref name="Xiao" /> | The beta hairpin stabilizes the <scene name='81/811707/Beta_hairpin_stabilizing_tyrs/1'>conformation of Tyr335 and Tyr337</scene>, while also shaping one side of the channel which the peptide binds to.<ref name="Xiao" /> The <scene name='81/811707/Peptide_binding_site/1'>peptide binding groove</scene> is composed of residues 255-268.<ref name="Xiao" /> Lysine would have trouble coming down into the active site in its charged form, but it is facilitated by the faces of the flanking tyrosines.<ref name="Xiao" /> The orientation of the lysine is such that the amine-methyl bond is aligned towards the sulfur on SAM so that it can provide the methyl. There is an important water in the active site (Figure 2) as well that acts as a stabilizer for lysine, and helps to shift the lone pair on the nitrogen towards the sulfur of SAM. <ref name="Xiao" /> | ||
[[Image:Hat1.gif|300 px|left|thumb|Figure X: The substrate ( | [[Image:Hat1.gif|300 px|left|thumb|Figure X: The substrate (pink sticks) and Coenzyme A (green sticks) binding channel in Hat1]] | ||
== Function == | == Function == | ||
