Sandbox Reserved 1074

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== '''Structure''' ==
== '''Structure''' ==
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Crystal structures of InhA reveal a <scene name='69/694241/Homotetramer_subunits_labeled/1'>homotetramer</scene> (each subunit featured with a different color) in aqueous solution with separate ligand binding sites in each subunit. Each <scene name='69/694241/Monomer_subunit_no_ligands/1'>monomer</scene> subunit is composed of 289 residues and features a typical [http://en.wikipedia.org/wiki/Rossmann_fold] containing a single NADH binding site. The <scene name='69/694241/Secondary_structure/1'>secondary structure</scene> of InhA is made up of several alpha helices (pink), beta sheets (gold), and beta turns (white). This enzyme also features a fatty acyl binding crevice that accommodates the long-chain fatty acyl substrate (2TK) needed to synthesize mycolic acid precursors. The <scene name='69/694241/Helix6_helix7_updated/1'>alpha-6 and alpha-7 helices</scene> of the InhA form one side of the fatty acyl binding crevice, referred to as the <scene name='69/694241/Monomer_subunit_196_219/1'> substrate binding loop (residues 196-219)</scene>.
Crystal structures of InhA reveal a <scene name='69/694241/Homotetramer_subunits_labeled/1'>homotetramer</scene> (each subunit featured with a different color) in aqueous solution with separate ligand binding sites in each subunit. Each <scene name='69/694241/Monomer_subunit_no_ligands/1'>monomer</scene> subunit is composed of 289 residues and features a typical [http://en.wikipedia.org/wiki/Rossmann_fold] containing a single NADH binding site. The <scene name='69/694241/Secondary_structure/1'>secondary structure</scene> of InhA is made up of several alpha helices (pink), beta sheets (gold), and beta turns (white). This enzyme also features a fatty acyl binding crevice that accommodates the long-chain fatty acyl substrate (2TK) needed to synthesize mycolic acid precursors. The <scene name='69/694241/Helix6_helix7_updated/1'>alpha-6 and alpha-7 helices</scene> of the InhA form one side of the fatty acyl binding crevice, referred to as the <scene name='69/694241/Monomer_subunit_196_219/1'> substrate binding loop (residues 196-219)</scene>.

Revision as of 18:39, 7 April 2015

This Sandbox is Reserved from 02/09/2015, through 05/31/2016 for use in the course "CH462: Biochemistry 2" taught by Geoffrey C. Hoops at the Butler University. This reservation includes Sandbox Reserved 1051 through Sandbox Reserved 1080.
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Enoyl-ACP Reductase InhA from Mycobacterium tuberculosis

Enoyl-ACP Reductase InhA Homotetramer

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References

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