User:John S. de Banzie/Sandbox 2

From Proteopedia

< User:John S. de Banzie(Difference between revisions)
Jump to: navigation, search
Current revision (19:27, 13 June 2014) (edit) (undo)
m
 
(18 intermediate revisions not shown.)
Line 1: Line 1:
-
==Carboxypeptidase A with Substrate==
+
==Zinc Finger==
-
<StructureSection load='3cpa' size='400' side='right' caption='Carboxypeptidase A with the dipeptide Gly-Tyr in the active site, [[3cpa]]' scene='59/590622/3cpaspacefill/2'>
+
<StructureSection load='1mey' size='400' side='right' caption='Leucine Zipper, [[1mey]]' scene='59/590622/1meyspacefill/1'>
-
Carboxypeptidase A catalyses the release of the C-terminal amino acid from a polypeptide chain. The initial image shows carboxypeptidase with a dipeptide (green) in the active site.
+
This zinc finger protein has one subunit. <scene name='59/590622/1meyspacefillunits/1'>Three zinc finger motifs</scene> fit into a major groove in the DNA. Each consists of an <scene name='59/590622/1meycartoon/1'>alpha helix, two short segments of beta pleated sheet, and a zinc ion (violet)</scene>.
-
 
+
-
The enzyme has <scene name='59/590622/3cpacartoon/1'>mixed secondary structure</scene>. A zinc ion (violet) is present. The ion is involved in binding and catalysis.
+
-
 
+
-
Substrate binding involves three interactions between the substrate and the active site.
+
-
 
+
-
1. <scene name='59/590622/3cpabindone/1'>Between the carbonyl group of the penultimate residue in the substrate and the zinc ion and an arginyl residue in the enzyme</scene>.
+
-
 
+
-
2. <scene name='59/590622/3cpabindtwo/1'>Between the C-terminal carboxyl group and asparaginyl, arginyl, and tyrosyl residues in the enzyme</scene>.
+
-
 
+
-
3. <scene name='59/590622/3cpabindthree/1'>Between the C-terminal R group and a hydrophobic pocket in the enzyme</scene>.
+
-
 
+
-
Catalysis involves <scene name='59/590622/3cpacatalysis/1'>electron withdrawal from the carbonyl of the penultimate residue by the zinc ion and an arginyl residue, and nucleophilic attack on that same group by a glutamyl residue</scene>.
+
-
 
+
-
(The substrate remained intact because Gly-Tyr is hydrolyzed very slowly and because X-ray crystallography was carried out at -9° C.)
+
</StructureSection>
</StructureSection>
== References ==
== References ==
<references/>
<references/>

Current revision

Zinc Finger

Leucine Zipper, 1mey

Drag the structure with the mouse to rotate

References

Proteopedia Page Contributors and Editors (what is this?)

John S. de Banzie

Retrieved from "http://52.214.119.220/wiki/index.php/User:John_S._de_Banzie/Sandbox_2"
Personal tools