2qj0: Difference between revisions
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|PDB= 2qj0 |SIZE=350|CAPTION= <scene name='initialview01'>2qj0</scene>, resolution 2.65Å | |PDB= 2qj0 |SIZE=350|CAPTION= <scene name='initialview01'>2qj0</scene>, resolution 2.65Å | ||
|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= UFD2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | |GENE= UFD2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[2qiz|2QIZ]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2qj0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qj0 OCA], [http://www.ebi.ac.uk/pdbsum/2qj0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2qj0 RCSB]</span> | |||
}} | }} | ||
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[[Category: ligase]] | [[Category: ligase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:49:49 2008'' | ||
Revision as of 01:49, 31 March 2008
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| 2qj0, resolution 2.65Å | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Ligands: | MSE | ||||||||||||
| Gene: | UFD2 (Saccharomyces cerevisiae) | ||||||||||||
| Related: | 2QIZ
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Structure of the yeast U-box-containing ubiquitin ligase Ufd2p
Overview
Proteins conjugated by Lys-48-linked polyubiquitin chains are preferred substrates of the eukaryotic proteasome. Polyubiquitination requires an activating enzyme (E1), a conjugating enzyme (E2), and a ligase (E3). Occasionally, these enzymes only assemble short ubiquitin oligomers, and their extension to full length involves a ubiquitin elongating factor termed E4. Ufd2p, as the first E4 identified to date, is involved in the degradation of misfolded proteins of the endoplasmic reticulum and of a ubiquitin-beta-GAL fusion substrate in Saccharomyces cerevisiae. The mechanism of action of Ufd2p is unknown. Here we describe the crystal structure of the full-length yeast Ufd2p protein. Ufd2p has an elongated shape consisting of several irregular Armadillo-like repeats with two helical hairpins protruding from it and a U-box domain flexibly attached to its C terminus. The U-box of Ufd2p has a fold similar to that of the RING (Really Interesting New Gene) domain that is present in certain ubiquitin ligases. Accordingly, Ufd2p has all of the hallmarks of a RING finger-containing ubiquitin ligase: it associates with its cognate E2 Ubc4p via its U-box domain and catalyzes the transfer of ubiquitin from the E2 active site to Ufd2p itself or to an acceptor ubiquitin molecule to form unanchored diubiquitin oligomers. Thus, Ufd2p can function as a bona fide E3 ubiquitin ligase to promote ubiquitin chain elongation on a substrate.
About this Structure
2QJ0 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Inaugural Article: Structure and function of the yeast U-box-containing ubiquitin ligase Ufd2p., Tu D, Li W, Ye Y, Brunger AT, Proc Natl Acad Sci U S A. 2007 Oct 2;104(40):15599-606. Epub 2007 Sep 21. PMID:17890322
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