Sandbox Reserved 982

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
{{Telford_CHEM321}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE -->
{{Telford_CHEM321}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE -->
-
==Your Heading Here (maybe something like 'Structure')==
+
==Shiga Toxin==
<StructureSection load='1R4Q' size='340' side='right' caption='Crystal Structure for Shiga Toxin (1R4Q)' scene=''>
<StructureSection load='1R4Q' size='340' side='right' caption='Crystal Structure for Shiga Toxin (1R4Q)' scene=''>
-
== Structure ==
+
== Structural Highlights ==
<scene name='68/687332/Shiga_toxin/5'>Crystal Structure of Shiga Toxin</scene>
<scene name='68/687332/Shiga_toxin/5'>Crystal Structure of Shiga Toxin</scene>
Stx is composed of two main subunits labeled A and B. The A subunit bonds noncovalently to the B subunit. The A subunit is 293 amino acids long with its active site being glutamic acid 167. Studies have shown that the first 239 residues are essential for the enzymatic activity of the A subunit. The B subunit is a pentamer that resembles a star and can be divided into five identical subunits. Each of the subunits is 69 amino acids in length. The purpose of the B subunit is to bind to globotriaosylceramide (GB3) which is a glycosphingolipid that resides on the surface of some Eukaryotic cells. Each monomer of the B subunit has three binding sites for GB3 making the protein very potent (Melton-Celsa 2013).
Stx is composed of two main subunits labeled A and B. The A subunit bonds noncovalently to the B subunit. The A subunit is 293 amino acids long with its active site being glutamic acid 167. Studies have shown that the first 239 residues are essential for the enzymatic activity of the A subunit. The B subunit is a pentamer that resembles a star and can be divided into five identical subunits. Each of the subunits is 69 amino acids in length. The purpose of the B subunit is to bind to globotriaosylceramide (GB3) which is a glycosphingolipid that resides on the surface of some Eukaryotic cells. Each monomer of the B subunit has three binding sites for GB3 making the protein very potent (Melton-Celsa 2013).
== Function ==
== Function ==
The pathway of stx entering a cell begins with the B subunit’s binding to GB3. Once this occurs, the A subunit disconnects from the B subunit and enters the cell through endocytosis. Using retrograde transport the A subunit passes through the Golgi apparatus and the rough endoplasmic reticulum. In the rough endoplasmic reticulum, the A subunit is cleaved into two parts called A1 and A2. A2 is degraded, but A1 freely enters the cytosol (Sandvig 2000). Once in the cytosol, A1 acts as an N-glycosidase, which is an enzyme that hydrolyzes bonds that link sugars. With this enzymatic activity, A1 removes adenines from the 28S RNA of the 60S ribosomal subunit (Melton-Celsa 2013). This inhibits protein synthesis and ultimately leads to cell death.
The pathway of stx entering a cell begins with the B subunit’s binding to GB3. Once this occurs, the A subunit disconnects from the B subunit and enters the cell through endocytosis. Using retrograde transport the A subunit passes through the Golgi apparatus and the rough endoplasmic reticulum. In the rough endoplasmic reticulum, the A subunit is cleaved into two parts called A1 and A2. A2 is degraded, but A1 freely enters the cytosol (Sandvig 2000). Once in the cytosol, A1 acts as an N-glycosidase, which is an enzyme that hydrolyzes bonds that link sugars. With this enzymatic activity, A1 removes adenines from the 28S RNA of the 60S ribosomal subunit (Melton-Celsa 2013). This inhibits protein synthesis and ultimately leads to cell death.
-
== Disease ==
+
== Function ==
-
== Relevance ==
+
== Disease and It's Pathogenesis ==
-
== Structural highlights ==
 
This is a sample scene created with SAT to <scene name='68/687332/Scene_1/1'>TextToBeDisplayed</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.
This is a sample scene created with SAT to <scene name='68/687332/Scene_1/1'>TextToBeDisplayed</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.

Revision as of 03:53, 1 May 2015

This Sandbox is Reserved from 15-Jan-2015, through 30-May-2015 for use in the course "Biochemistry" taught by Jason Telford at the Maryville University. This reservation includes Sandbox Reserved 977 through Sandbox Reserved 986.
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

Shiga Toxin

Crystal Structure for Shiga Toxin (1R4Q)

Drag the structure with the mouse to rotate

References

Personal tools