CED-4 Apoptosome: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
New page: left|200px <!-- The line below this paragraph, containing "STRUCTURE_3lqq", creates the "Structure Box" on the page. You may change the PDB parameter (which sets the PD...
 
No edit summary
Line 1: Line 1:
<StructureSection load="3lqq" size="400" color="" frame="true"  spin="on" Scene='3lqq/Default/1'  align="right" caption= >
[[Image:3lqq.jpg|left|200px]]
[[Image:3lqq.jpg|left|200px]]
 
===Structure of the CED-4 Apoptosome ([[3lqq]])===
<!--
The line below this paragraph, containing "STRUCTURE_3lqq", creates the "Structure Box" on the page.
You may change the PDB parameter (which sets the PDB file loaded into the applet)
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
or leave the SCENE parameter empty for the default display.
-->
{{STRUCTURE_3lqq|  PDB=3lqq  |  SCENE=3lqq/Default/1  |CAPTION= 3lqq asymmetric unit, resolution 3.53&Aring;. <br> Click <scene name='3lqq/Biomolecule1/4'>here</scene> to display biological molecule.}}
 
 
===Structure of the CED-4 Apoptosome===
{{ABSTRACT_PUBMED_20434985}}
{{ABSTRACT_PUBMED_20434985}}
<!--
<!--
Line 24: Line 15:


==About this Structure==
==About this Structure==
3LQQ is a 2 chains structure with sequences from [http://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LQQ OCA].  
[[3lqq]] is a 2 chains structure with sequences from [http://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LQQ OCA].  


<scene name='3lqq/Default/1'>The crystallographic asymmetric unit of the solved structure is an asymmetric dimer</scene> of CED-4.  <scene name='3lqq/Morph/2'>Morph showing how each monomer in the asymmetric dimer relate to each other</scene>. Be sure to spin it around because <scene name='3lqq/Morphside/3'>from the side it is easier to see the dramatic difference</scene>.<br> {{Button Toggle AnimationOnPause}}<!--When Proteopedia updates to a version of Jmol that supports the Compare command, I should upload a new pdb file with chain as a model and chain b as a model in a single pdb file and then replace this scene with a scripted compare that just compares model 2 (chain b) to model 1 (chain a).-->
<scene name='3lqq/Default/1'>The crystallographic asymmetric unit of the solved structure is an asymmetric dimer</scene> of CED-4.  <scene name='3lqq/Morph/2'>Morph showing how each monomer in the asymmetric dimer relate to each other</scene>. Be sure to spin it around because <scene name='3lqq/Morphside/3'>from the side it is easier to see the dramatic difference</scene>.<br> {{Button Toggle AnimationOnPause}}<!--When Proteopedia updates to a version of Jmol that supports the Compare command, I should upload a new pdb file with chain as a model and chain b as a model in a single pdb file and then replace this scene with a scripted compare that just compares model 2 (chain b) to model 1 (chain a).-->


<scene name='3lqq/Biomolecule1/4'>The biological molecule is an octamer (tetramer of the asymmetric dimer)</scene> that forms a shape similar to a funnel.<br>
<scene name='3lqq/Biomolecule1/4'>The biological molecule is an octamer (tetramer of the asymmetric dimer)</scene> that forms a shape similar to a funnel.<br>
{{Link Toggle FancyCartoonHighQualityView}}.
 
==External Links==
==External Links==
* [http://www.nature.com/nchina/2010/100707/full/nchina.2010.77.html '''Structural biology: The funnel of death''' by Felix Cheung] at Nature China.
* [http://www.nature.com/nchina/2010/100707/full/nchina.2010.77.html '''Structural biology: The funnel of death''' by Felix Cheung] at Nature China.
Line 45: Line 36:
[[Category: Mitochondrion]]
[[Category: Mitochondrion]]
[[Category: Nucleotide-binding]]
[[Category: Nucleotide-binding]]
<br />
Created with the participation of [[User:Wayne Decatur|Wayne Decatur]], [[User:Eran Hodis|Eran Hodis]].

Revision as of 16:00, 13 June 2012

<StructureSection load="3lqq" size="400" color="" frame="true" spin="on" Scene='3lqq/Default/1' align="right" caption= >

Structure of the CED-4 Apoptosome (3lqq)Structure of the CED-4 Apoptosome (3lqq)

Publication Abstract from PubMed

The CED-4 homo-oligomer or apoptosome is required for initiation of programmed cell death in Caenorhabditis elegans by facilitating autocatalytic activation of the CED-3 caspase zymogen. How the CED-4 apoptosome assembles and activates CED-3 remains enigmatic. Here we report the crystal structure of the complete CED-4 apoptosome and show that it consists of eight CED-4 molecules, organized as a tetramer of an asymmetric dimer via a previously unreported interface among AAA(+) ATPases. These eight CED-4 molecules form a funnel-shaped structure. The mature CED-3 protease is monomeric in solution and forms an active holoenzyme with the CED-4 apoptosome, within which the protease activity of CED-3 is markedly stimulated. Unexpectedly, the octameric CED-4 apoptosome appears to bind only two, not eight, molecules of mature CED-3. The structure of the CED-4 apoptosome reveals shared principles for the NB-ARC family of AAA(+) ATPases and suggests a mechanism for the activation of CED-3.

Crystal structure of the Caenorhabditis elegans apoptosome reveals an octameric assembly of CED-4., Qi S, Pang Y, Hu Q, Liu Q, Li H, Zhou Y, He T, Liang Q, Liu Y, Yuan X, Luo G, Li H, Wang J, Yan N, Shi Y, Cell. 2010 Apr 30;141(3):446-57. PMID:20434985

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this StructureAbout this Structure

3lqq is a 2 chains structure with sequences from Caenorhabditis elegans. Full crystallographic information is available from OCA.

of CED-4. . Be sure to spin it around because .


that forms a shape similar to a funnel.

External LinksExternal Links


Created with the participation of Wayne Decatur, Eran Hodis.

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Alexander Berchansky, Michal Harel