Sandbox Reserved 1056: Difference between revisions
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== Structure == | == Structure == | ||
[[Image:homotetramer.png|150 px|left|thumb|Figure 2: 222 Symmetry of the homotetramer isocitrate lyase. Each identical monomer is shown in a unique color.]] | [[Image:homotetramer.png|150 px|left|thumb|Figure 2: 222 Symmetry of the homotetramer isocitrate lyase. Each identical monomer is shown in a unique color.]] | ||
The ICL homotetramer possesses 222 symmetry, with an axis of rotation | The ICL homotetramer possesses 222 symmetry, with an axis of rotation about the x-axis, y-axis, and z-axis of the enzyme. Two individual subunits of ICL, shown here as blue and green, are held together by a characteristic <scene name='69/697526/Helix_swapping/3'>Helix Swapping</scene> between three alpha helices formed by residues 370-384, 349-367, and 399-409 on neighboring monomers<ref name="ICL">PMID:10932251</ref>. The interlocking mechanism created by these helices provides additional strength to hold the two monomeric subunits together, allowing ICL to be composed of a dimer of dimers<ref name="ICL2"/>. This interaction will bury approximately 18% of the surface of each subunit, and will help to shield the interior binding site from hydration. | ||
== Active Site == | == Active Site == | ||