Sandbox Reserved 1074

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{{Sandbox_Reserved_Butler_CH462_Sp2015_#}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE -->
{{Sandbox_Reserved_Butler_CH462_Sp2015_#}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE -->
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==Your Protein Name here==
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<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
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This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
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You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
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=='''Enoyl-ACP Reductase InhA from ''Mycobacterium tuberculosis'''''==
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== Biological Function ==
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<StructureSection load='4OHU' size='340' side='right' caption='Enoyl-ACP Reductase InhA Homotetramer'>
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== Structural Overview ==
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== '''Introduction''' ==
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== Mechanism of Action ==
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=== '''FAS-II System''' ===
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== Zinc Ligand(s) ==
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=== '''Mechanism of Action''' ===
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== Other Ligands ==
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This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
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== '''General Structural Information''' ==
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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 Rossmann fold] containing a single NADH binding site. The <scene name='69/694241/Secondary_structure_black/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 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</scene> (residues 196-219). [[Image:Fatty Acyl Binding Crevice.jpg|thumb|200px|left|Fatty Acyl Binding Crevice (substrate binding loop in purple; substrates pictured inside the crevice)]] One side of this crevice is open and exposed to solvent, which allows the substrates to access the binding pocket of this enzyme. The size of the substrate binding loop is a primary determinant of the ability of InhA to select for fatty acyl chains longer than 16 carbons to successfully produce mycolic acid precursors.
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Talk generally about catalytic triad. More specific details in sections below.
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=== '''Fatty Acyl Binding Crevice''' ===
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Within the fatty acyl binding crevice, the NADH substrate sits on the top shelf of the Rossmann fold, and the fatty acyl substrate sits on top of the NADH substrate. Both of these substrates are held in place through interactions with the side chains of <scene name='69/694241/Sbl_hydrophobic/1'>hydrophobic</scene> (purple) residues. The majority of these <scene name='69/694241/Hydrophobic_residues/1'>hydrophobic</scene> residues anchoring the substrates are found within the substrate binding loop itself, including Ala-198, Met-199, Ala-201, Ile-202, Leu-207, Ile-215, and Leu-218. [[Image:Binding Pocket - Mesh.jpg|thumb|250px|right|Substrate Binding Pocket (NADH in green; fatty acyl substrate in red)]] Studies have found that the fatty acyl substrate adopts a u-shaped conformation to facilitate binding.
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<scene name='69/694241/Nadh_fatty_acyl_substrate/2'>NADH and fatty acyl binding substrate</scene>
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=== '''Catalytic Triad''' ===
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<scene name='69/694241/Catalytic_triad/1'>catalytic triad</scene>
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[[Image:Tyr-158.jpg|thumb|200px|left|Tyr-158]]
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=== '''Hydrogen Bonding Interactions''' ===
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<scene name='69/694241/Monomer_subunit/2'>NADH binding site</scene>.
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<scene name='69/697507/Fatty_acyl_binding_crevice/3'>Space-Filled Model of Atoms in Fatty Acyl Binding Crevice</scene>
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== '''Clinical Applications''' ==
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This is a sample scene created with SAT to <scene name="69/697507/Fatty_acyl_binding_crevice/3">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
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</StructureSection>
</StructureSection>
== References ==
== References ==
<references/>
<references/>

Current revision

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.
To get started:
  • Click the edit this page tab at the top. Save the page after each step, then edit it again.
  • Click the 3D button (when editing, above the wikitext box) to insert Jmol.
  • show the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page.
  • Add a description of your scene. Use the buttons above the wikitext box for bold, italics, links, headlines, etc.

More help: Help:Editing

Your Protein Name here

Caption for this structure

Drag the structure with the mouse to rotate

References

  1. ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
  2. ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
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