Sandbox Reserved 1058: Difference between revisions
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===Structure=== | ===Structure=== | ||
[[Image:Normal_Crystal_Structure.png|250 px|center|thumb|'''Figure 1. Crystal Structure of Isocitrate Lyase.''' Quaternary structure is comprised of four subunits forming an alpha/beta barrel.]] | [[Image:Normal_Crystal_Structure.png|250 px|center|thumb|'''Figure 1. Crystal Structure of Isocitrate Lyase.''' Quaternary structure is comprised of four subunits forming an alpha/beta barrel.]] | ||
[http://www.rcsb.org/pdb/explore/explore.do?structureId=1f8i Isocitrate lyase] is a tetramer with 222 symmetry. Each subunit is composed of 14 alpha helices and 14 beta sheets which includes a total of 426 residues. These α helices and β sheets form an unusual α/β barrel seen in Figure 1. The α/β barrel contains a topology of (βα)<sub>2</sub>α(βα)<sub>5</sub>β, differing from the canonical (βα)<sub>8</sub> pattern. Residues 184-200 and 235-254 connects the third and forth β-strands to their consecutive helices and form a small β-domain that consists of a short five-stranded βsheet(β6,β7,β9,β10,β11) that lies on top of the α/β barrel.*GREEN LINK MOTHERFUCKER* | [http://www.rcsb.org/pdb/explore/explore.do?structureId=1f8i Isocitrate lyase] is a tetramer with 222 symmetry. Each subunit is composed of 14 alpha helices and 14 beta sheets which includes a total of 426 residues. These α helices and β sheets form an unusual α/β barrel seen in Figure 1. The α/β barrel contains a topology of (βα)<sub>2</sub>α(βα)<sub>5</sub>β, differing from the canonical (βα)<sub>8</sub> pattern. Residues 184-200 and 235-254 connects the third and forth β-strands to their consecutive helices and form a small β-domain that consists of a short five-stranded βsheet (β6,β7,β9,β10,β11) that lies on top of the α/β barrel.*GREEN LINK MOTHERFUCKER* Isocitrate Lyase shows a resemblance to [http://www.rcsb.org/pdb/explore/explore.do?structureId=1S2V phosphoenolpyrvate mutase] | ||
===Helix Swapping=== | ===Helix Swapping=== | ||
A unique structural feature of this enzyme is a phenomenon called "<scene name='69/694225/Helix_swapping/1'>helix swapping</scene>". | A unique structural feature of this enzyme is a phenomenon called "<scene name='69/694225/Helix_swapping/1'>helix swapping</scene>". | ||
