Sandbox Reserved 1656: Difference between revisions
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3TMP is the catalytic domain of human deubiquitinase DUBA in complex with ubiquitin aldehyde. It is a 8 chain structure with sequence from Human. Indeed, 3TMP is made of these two macromolecules : OTU domain-containing protein 5 ( also named DUBA or OTUD5) and Polyubiquitin-C, which is the ubiquitin aldehyde. It is also made of two small molecules which are the phosphoserine (SEP) and the amino-acetaldehyde (GLZ), they are L-peptide links. <ref>PMID:22245969</ref> | 3TMP is the catalytic domain of human deubiquitinase DUBA in complex with ubiquitin aldehyde. It is a 8 chain structure with sequence from Human. Indeed, 3TMP is made of these two macromolecules : OTU domain-containing protein 5 ( also named DUBA or OTUD5) and Polyubiquitin-C, which is the ubiquitin aldehyde. It is also made of two small molecules which are the phosphoserine (SEP) and the amino-acetaldehyde (GLZ), they are L-peptide links. <ref>PMID:22245969</ref> | ||
=== Impact of phosphorylation on DUB activity === | |||
Evidence shows that phosphorylation influences activity of the enzyme. Phosphorylated serine seems to have the most influence on the activity of the enzyme <scene name='86/868189/Ser177/1'>especially on Ser177</scene>. The phosphorylation of this nucleotide is crucial and the protein won't work if it's not. | |||
In fact, this part bends to welcome the protein to be deubiquitinased. | |||
==== Catalytic domain ==== | ==== Catalytic domain ==== | ||
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Residues present in the catalytic site of DUBs are often in a '''non-functional orientation''' when the substrate is absent. Thus, when the substrate binds to the catalytic site of the enzyme, the site undergoes rearrangement and takes on a functional conformation. <ref>PMID:16537382</ref> The substrate opens and closes to allow the entry of the protein to be deubiquitinased. | Residues present in the catalytic site of DUBs are often in a '''non-functional orientation''' when the substrate is absent. Thus, when the substrate binds to the catalytic site of the enzyme, the site undergoes rearrangement and takes on a functional conformation. <ref>PMID:16537382</ref> The substrate opens and closes to allow the entry of the protein to be deubiquitinased. | ||
== Biological role == | == Biological role == | ||
