Sandbox Reserved 975: Difference between revisions

Revision as of 14:45, 31 December 2014

This Sandbox is Reserved from 15/11/2014, through 15/05/2015 for use in the course "Biomolecule" taught by Bruno Kieffer at the Strasbourg University. This reservation includes Sandbox Reserved 951 through Sandbox Reserved 975.

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ContextContext

The SUMO-conjugating enzyme UBC9 is involved in ubiquitination of proteins.

The Ubiquitin is a small protein of 76 aa.

Ubiquitination is a post translationnal modification where an ubiquitin is attached to a protein. This modification has several consequences, it can lead to the degradation of the protein via the proteasome, it can change the protein localization or it can alter the interaction of the protein with other factors, this is why this modification plays an important role in the control of many cellular processes.

UBC9 in particular is important in the cell cycle progression because it allows the degradation of S phase and M phase cyclines.

Ubiquitination occurs in three steps : Activation performed by ubiquitin-activating enzymes E1, conjugation performed by ubiquitin-conjugating enzymes E2 and ligation performed by ubiquitin ligases E3.

During the first step the Ct Carboxyl group of the ubiquitin is linked to the cystein sulfhydryl group of E1.

The second step is a transesterification to transfer the active ubiquitin from the cystein of E1 to the cystein of E2. E2 binds the activated ubiquitin and E1.

During the third step E3 catalyses the formation of an isopeptide bond between a lysine of the substrate and a glycine of the ubiquitin.

UBC9 is a E2. It is a lynchpin in the SUMO pathway, it interacts with E1 during the activation, then with the ubiquitin after the transfer and finally with E3 during conjugation. It is particularly important for the formation of polymeric chain when the number of SUMO exceeds 2.

Structure

Function

Interaction with the substrates

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ReferencesReferences

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA, Manon Camaille, Elsa Gambs

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 ==Context==
 <StructureSection load='1uin' size='340' side='right' caption='Caption for this structure' scene=''>
-This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
+The SUMO-conjugating enzyme UBC9 is involved in ubiquitination of proteins.
-You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
+The Ubiquitin is a small protein of 76 aa.
+Ubiquitination is a post translationnal modification where an ubiquitin is attached to a protein. This modification has several consequences, it can lead to the degradation of the protein via the proteasome, it can change the protein localization or it can alter the interaction of the protein with other factors, this is why this modification plays an important role in the control of many cellular processes.
+UBC9 in particular is important in the cell cycle progression because it allows the degradation of S phase and M phase cyclines.
+Ubiquitination occurs in three steps : Activation performed by ubiquitin-activating enzymes E1, conjugation performed by ubiquitin-conjugating enzymes E2 and ligation performed by ubiquitin ligases E3.
+During the first step the Ct Carboxyl group of the ubiquitin is linked to the cystein sulfhydryl group of E1.
+The second step is a transesterification to transfer the active ubiquitin from the cystein of E1 to the cystein of E2. E2 binds the activated ubiquitin and E1.
+During the third step E3 catalyses the formation of an isopeptide bond between a lysine of the substrate and a glycine of the ubiquitin.
+UBC9 is a E2. It is a lynchpin in the SUMO pathway, it interacts with E1 during the activation, then with the ubiquitin after the transfer and finally with E3 during conjugation. It is particularly important for the formation of polymeric chain when the number of SUMO exceeds 2.
 == Structure ==