6dxh

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Structure of USP5 zinc-finger ubiquitin binding domain co-crystallized with 4-(4-tert-butylphenyl)-4-oxobutanoateStructure of USP5 zinc-finger ubiquitin binding domain co-crystallized with 4-(4-tert-butylphenyl)-4-oxobutanoate

Structural highlights

6dxh is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, ,
Activity:Ubiquitinyl hydrolase 1, with EC number 3.4.19.12
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[UBP5_HUMAN] Cleaves linear and branched multiubiquitin polymers with a marked preference for branched polymers. Involved in unanchored 'Lys-48'-linked polyubiquitin disassembly. Binds linear and 'Lys-63'-linked polyubiquitin with a lower affinity. Knock-down of USP5 causes the accumulation of p53/TP53 and an increase in p53/TP53 transcriptional activity because the unanchored polyubiquitin that accumulates is able to compete with ubiquitinated p53/TP53 but not with MDM2 for proteasomal recognition.[1]

See Also

References

  1. Dayal S, Sparks A, Jacob J, Allende-Vega N, Lane DP, Saville MK. Suppression of the deubiquitinating enzyme USP5 causes the accumulation of unanchored polyubiquitin and the activation of p53. J Biol Chem. 2009 Feb 20;284(8):5030-41. doi: 10.1074/jbc.M805871200. Epub 2008, Dec 19. PMID:19098288 doi:http://dx.doi.org/10.1074/jbc.M805871200

6dxh, resolution 2.00Å

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OCA