Calmodulin

From Proteopedia

(Difference between revisions)

@@ Line 20: / Line 20: @@
 <jmolButton>
 <script>
-script "/wiki/images/1/1a/Morph.spt";
+script "/wiki/images/a/a2/Storymorph.spt";
 load files "=1prw" "=1cll";
 delete water;
@@ Line 41: / Line 41: @@
 structures = [{1.1}, {2.1}];
 my_recipe = [
-[0, 1, 0, {79-147},{79-147}, {(79-138) and alpha}, 0],
+[{79-147},{79-147}, {(79-138) and alpha}],
-[0, 1, 0, {4-78}, {79}, {(8-78) and alpha}, 0],
+[{4-78}, {79}, {(8-78) and alpha}],
 ];
-morph(20, structures, my_recipe, 0);
+morph(20, structures, my_recipe);
 </script>
 <text>Open</text>
@@ Line 57: / Line 57: @@
 structures = [{2.1}, {1.1}];
 my_recipe = [
-[0, 1, 0, {79-147},{79-147}, {(79-138) and alpha}, 0],
+[{79-147},{79-147}, {(79-138) and alpha}],
-[0, 1, 0, {4-78}, {79}, {(8-78) and alpha}, 0],
+[{4-78}, {79}, {(8-78) and alpha}],
 ];
-morph(20, structures, my_recipe, 0);
+morph(20, structures, my_recipe);
 </script>
 <text>Close</text>
@@ Line 70: / Line 70: @@
 <jmolButton>
 <script>
-script "/wiki/images/1/1a/Morph.spt";
+script "/wiki/images/a/a2/Storymorph.spt";
 load files "=1prw" "=1cll";
 delete water;
@@ Line 91: / Line 91: @@
 structures = [{1.1}, {2.1}];
 my_recipe = [
-[0, 1, 0, {79-147},{79-147}, {(79-138) and alpha}, 0],
+[{79-147},{79-147}, {(79-138) and alpha}],
-[0, 1, 0, {4-78}, {79}, {(8-78) and alpha}, 0],
+[{4-78}, {79}, {(8-78) and alpha}],
 ];
-morph(20, structures, my_recipe, 0);
+morph(20, structures, my_recipe);
 </script>
 <text>Open</text>
@@ Line 107: / Line 107: @@
 structures = [{2.1}, {1.1}];
 my_recipe = [
-[0, 1, 0, {79-147},{79-147}, {(79-138) and alpha}, 0],
+[{79-147},{79-147}, {(79-138) and alpha}],
-[0, 1, 0, {4-78}, {79}, {(8-78) and alpha}, 0],
+[{4-78}, {79}, {(8-78) and alpha}],
 ];
-morph(20, structures, my_recipe, 0);
+morph(20, structures, my_recipe);
 </script>
 <text>Close</text>
@@ Line 120: / Line 120: @@
 <jmolButton>
 <script>
-script "/wiki/images/1/1a/Morph.spt";
+script "/wiki/images/a/a2/Storymorph.spt";
 load files "=1prw" "=1cll";
 delete water;
@@ Line 141: / Line 141: @@
 structures = [{1.1}, {2.1}];
 my_recipe = [
-[0, 1, 0, {4-78}, {4-78}, {(8-78) and alpha}, 0],
+[{4-78}, {4-78}, {(8-78) and alpha}],
-[0, 1, 0, {79-147},{78}, {(79-138) and alpha}, 0],
+[{79-147},{78}, {(79-138) and alpha}],
 ];
-morph(20, structures, my_recipe, 0);
+morph(20, structures, my_recipe);
 </script>
 <text>Open</text>
@@ Line 157: / Line 157: @@
 structures = [{2.1}, {1.1}];
 my_recipe = [
-[0, 1, 0, {4-78}, {4-78}, {(8-78) and alpha}, 0],
+[{4-78}, {4-78}, {(8-78) and alpha}],
-[0, 1, 0, {79-147},{78}, {(79-138) and alpha}, 0],
+[{79-147},{78}, {(79-138) and alpha}],
 ];
-morph(20, structures, my_recipe, 0);
+morph(20, structures, my_recipe);
 </script>
 <text>Close</text>

Current revision

spinqualitylabelsall models

Human calmodulin complex with ethanol and Ca+2 ions (green) (PDB code 1cll)

Show:Asymmetric Unit Biological Assembly

Drag the structure with the mouse to rotate

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1 Function
2 Maximum Occurrence of Calmodulin Conformations
3 Calmodulin in Motion
4 3D Structures of Calmodulin

Function

Calmodulin (CaM) – calcium modulated protein – regulates various protein targets. It is used by various proteins as calcium sensor and signal transducer by binding to their calcium binding domain (CBD). It undergoes conformational change upon binding Ca++ via its 4 EF hand motives and can undergo post-translational modification. of Human calmodulin (PDB code 1cll). ^[1] More details on apo-CaM Calcium-free Calmodulin and Calmodulin JMU.

Maximum Occurrence of Calmodulin Conformations

Maximum Occurrence, a method for making rigorous numerical assessments about the maximum percent of time that a conformer of a flexible macromolecule can exist and still be compatible with the experimental data, was used to probe the conformational disorder of Calmodulin^[2].

Figure 3: Orientation tensor representation for 400 conformational states of Calmodulin, color coded according to their MO values (from less than 5% in blue to more than 30% in red).To better explain their meaning, 10 randomly chosen models are shown as cartoons and then replaced by the three axes of their color-coded orientation tensors.

It was shown that the open (1cll) and closed (1prw) conformers can have MO of only 15% and 5% respectively.

Calmodulin in Motion

The buttons below allow you to explore morphs ^[3] between structures 1prw and 1cll.

The following morph is between 1prw and 1cll after superposition of residues 79-138. This shows the subtle conformational changes in that domain more clearly.

The following morph is between 1prw and 1cll after superposition of residues 8-78. This shows the subtle conformational changes in that domain more clearly.

3D Structures of Calmodulin

Calmodulin 3D structures

Bibliography

↑ Chattopadhyaya R, Meador WE, Means AR, Quiocho FA. Calmodulin structure refined at 1.7 A resolution. J Mol Biol. 1992 Dec 20;228(4):1177-92. PMID:1474585
↑ Bertini I, Giachetti A, Luchinat C, Parigi G, Petoukhov MV, Pierattelli R, Ravera E, Svergun DI. Conformational Space of Flexible Biological Macromolecules from Average Data. J Am Chem Soc. 2010 Sep 7. PMID:20822180 doi:10.1021/ja1063923
↑ The Storymorph Jmol scripts creates the interpolated coordinates of the morph on the fly.