Sandbox Reserved 1074

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 14: Line 14:
== '''Structure''' ==
== '''Structure''' ==
-
<scene name='69/694241/Secondary_structure/1'>secondary structure</scene>
+
<scene name='69/694241/Helix6_helix7/2'>TextToBeDisplayed</scene>
-
Crystal structures of InhA reveal a <scene name='69/694241/Homotetramer_subunits_labeled/1'>homotetramer</scene> (each subunit featured with a different color) with separate ligand binding sites in each subunit. Each <scene name='69/694241/Monomer_subunit_no_ligands/1'>monomer</scene> subunit features a single domain with a central core that supports a NADH binding site. The alpha6 and alpha7 helices of the monomer form one side of the fatty acyl substrate binding crevice of InhA. Within this binding crevice, many hydrophobic side chains from the amino acids involved in forming the substrate binding loop, <scene name='69/694241/Monomer_subunit_196_219/1'> residues 196-219</scene>, interact with the substrates. [[Image:Fatty Acyl Binding Crevice.jpg|thumb|200px|left|Fatty Acyl Binding Crevice]] One side of this cavity 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 distinguish between shorter and longer substrates and provide <scene name='69/694241/Substrate_binding_pocket/1'>specificity</scene> for the enoyl-ACP reductase reaction.
+
 
 +
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 alpha-6 and alpha-7 helices 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>.
 +
 
 +
 
 +
 
 +
interact with the substrates. [[Image:Fatty Acyl Binding Crevice.jpg|thumb|200px|left|Fatty Acyl Binding Crevice]] One side of this cavity 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 distinguish between shorter and longer substrates and provide <scene name='69/694241/Substrate_binding_pocket/1'>specificity</scene> for the enoyl-ACP reductase reaction.

Revision as of 17:57, 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.
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

Enoyl-ACP Reductase InhA from Mycobacterium tuberculosis

Enoyl-ACP Reductase InhA Homotetramer

Drag the structure with the mouse to rotate

References

Retrieved from "http://52.214.119.220/wiki/index.php/Sandbox_Reserved_1074"
Personal tools