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User:John S. de Banzie/Sandbox 2

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==Carboxypeptidase A==
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==Zinc Finger==
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<StructureSection load='4cpa' size='400' side='right' caption='Carboxypeptidase A, [[4cpa]]' scene='59/590622/4cpaspacefill/4'>
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<StructureSection load='1mey' size='400' side='right' caption='Leucine Zipper, [[1mey]]' scene='59/590622/1meyspacefill/1'>
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Carboxypeptidase A catalyses the release of the C-terminal amino acid from a polypeptide chain. The initial image shows carboxypeptidase with a tetrapeptide (green) bound in the active site.
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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>.
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The enzyme has <scene name='59/590622/4cpacartoon/2'>mixed secondary structure</scene>. A <scene name='59/590622/4cpacartoonzn/3'>zinc ion</scene> is present. The ion is involved in binding and catalysis.
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Substrate binding involves three interactions between the substrate and the active site.
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1. <scene name='59/590622/4cpabindone/3'>Between the carbonyl group of the penultimate residue in the substrate and the zinc ion and an arginyl residue in the enzyme</scene>.
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2. <scene name='59/590622/4cpabindtwo/2'>Between the C-terminal carboxyl group and asparaginyl, arginyl, and tyrosyl residues in the enzyme</scene>.
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3. <scene name='59/590622/4cpabindthree/2'>Between the C-terminal R group and a hydrophobic pocket in the enzyme</scene>.
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Catalysis involves <scene name='59/590622/4cpacatalysis/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>.
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</StructureSection>
</StructureSection>
== References ==
== References ==
<references/>
<references/>

Current revision

Zinc Finger

Leucine Zipper, 1mey

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References

Proteopedia Page Contributors and Editors (what is this?)

John S. de Banzie

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