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==Isocitrate Lyase== | ==Isocitrate Lyase== | ||
===Structure=== | ===Structure=== | ||
[[Image:Normal_Crystal_Structure.png|250 px| | [[Image:Normal_Crystal_Structure.png|250 px|left|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 <scene name='69/694225/Small_beta_domain/1'>small β-domain</scene> that consists of a short five-stranded βsheet (β6,β7,β9,β10,β11) that lies on top of the α/β barrel. <ref name="sharma"> Sharma, V.; Sharma, S.; Hoener zu Bentrup, K.; McKinney, J.; Russell, D.; ''et. al''; Structure of isocitrate lyase, a persistence factor of ''Mycobacterium tuberculosis''. ''Nat. Struct. Biol.''. '''2000'''. ''7(8)'':663-668. </ref> A study of the equilibria between the four subunits shows that each isocitrate lyase monomer has a dynamic comformational change of the active site loop. At any given time, only two of the subunits are in the open conformation. <ref name="gould"> Gould, T.; van de Langemheen, H.; Muñoz-Elías, E.; McKinney, D.; Sacchettini, J.; Dual role of isocitrate lyase 1 in the glyoxylate and methylcitrate cycles in ''Mycobacterium tuberculosis''. ''Molecular Microbiology''. '''2006'''. ''61(4)'':940-947. doi:10.1111/j.1365-2958.2006.05297.x. </ref> Isocitrate Lyase shows a resemblance to [http://www.rcsb.org/pdb/explore/explore.do?structureId=1S2V phosphoenolpyrvate mutase]. <ref name="sharma"> Sharma, V.; Sharma, S.; Hoener zu Bentrup, K.; McKinney, J.; Russell, D.; ''et. al''; Structure of isocitrate lyase, a persistence factor of ''Mycobacterium tuberculosis''. ''Nat. Struct. Biol.''. '''2000'''. ''7(8)'':663-668. </ref> | [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 <scene name='69/694225/Small_beta_domain/1'>small β-domain</scene> that consists of a short five-stranded βsheet (β6,β7,β9,β10,β11) that lies on top of the α/β barrel. <ref name="sharma"> Sharma, V.; Sharma, S.; Hoener zu Bentrup, K.; McKinney, J.; Russell, D.; ''et. al''; Structure of isocitrate lyase, a persistence factor of ''Mycobacterium tuberculosis''. ''Nat. Struct. Biol.''. '''2000'''. ''7(8)'':663-668. </ref> A study of the equilibria between the four subunits shows that each isocitrate lyase monomer has a dynamic comformational change of the active site loop. At any given time, only two of the subunits are in the open conformation. <ref name="gould"> Gould, T.; van de Langemheen, H.; Muñoz-Elías, E.; McKinney, D.; Sacchettini, J.; Dual role of isocitrate lyase 1 in the glyoxylate and methylcitrate cycles in ''Mycobacterium tuberculosis''. ''Molecular Microbiology''. '''2006'''. ''61(4)'':940-947. doi:10.1111/j.1365-2958.2006.05297.x. </ref> Isocitrate Lyase shows a resemblance to [http://www.rcsb.org/pdb/explore/explore.do?structureId=1S2V phosphoenolpyrvate mutase]. <ref name="sharma"> Sharma, V.; Sharma, S.; Hoener zu Bentrup, K.; McKinney, J.; Russell, D.; ''et. al''; Structure of isocitrate lyase, a persistence factor of ''Mycobacterium tuberculosis''. ''Nat. Struct. Biol.''. '''2000'''. ''7(8)'':663-668. </ref> | ||
