Sandbox Reserved 1656: Difference between revisions
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It is the '''catalytic domain''' which defines the family of the DUB. Indeed, DUBs belonging to the family of cysteine proteases have a catalytic site composed of two or three amino acids (dyads or triads). When the catalytic site is active, it may contain cysteine, histidine, aspartate or asparagine residues. In the case of metalloproteases, the active site is composed of a zinc ion and amino acids such as histidine, aspartate and serine. <ref>https://authors.library.caltech.edu/261/1/AMBpb04.pdf</ref> | It is the '''catalytic domain''' which defines the family of the DUB. Indeed, DUBs belonging to the family of cysteine proteases have a catalytic site composed of two or three amino acids (dyads or triads). When the catalytic site is active, it may contain cysteine, histidine, aspartate or asparagine residues. In the case of metalloproteases, the active site is composed of a zinc ion and amino acids such as histidine, aspartate and serine. <ref>https://authors.library.caltech.edu/261/1/AMBpb04.pdf</ref> | ||
The studied structure shows both <scene name='86/868189/Catalytic_site_polyubiquitine/2'>the catalytic site (in orange) and polyubiquitine in purple.</scene> | The studied structure shows both <scene name='86/868189/Catalytic_site_polyubiquitine/2'>the catalytic site (in orange) and polyubiquitine (in purple).</scene> | ||
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. | ||
The enzyme take this configuration thanks to <scene name='86/868189/H_bonds_around_ser177/1'>many hydrogen bonds around Ser177.</scene> This is why | The enzyme take this configuration thanks to <scene name='86/868189/H_bonds_around_ser177/1'>many hydrogen bonds around Ser177.</scene> This is why phosphorylation is so important to the function of the enzyme. The phosphate group forms many links between substrate ubiquitin and a segment of the OTU domain. This is rare among the known structures of deubiquitinases. Phosphorylation-driven conformational change ressembles the one of [https://en.wikipedia.org/wiki/Kinase kinases]. | ||
== Biological role == | == Biological role == | ||
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== References == | == References == | ||
<references/> | <references/> | ||
