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3M3J

A new crystal form of Lys48-linked diubiquitin

Summary for 3M3J
Entry DOI10.2210/pdb3m3j/pdb
DescriptorUbiquitin, 1,2-ETHANEDIOL, SULFATE ION, ... (4 entities in total)
Functional Keywordsbeta grasp, ubiquitin, isopeptide bond, nucleus, protein degradation, proteasome, signaling protein, lys48-linked
Biological sourceBos taurus (bovine,cow,domestic cattle,domestic cow)
Total number of polymer chains6
Total formula weight51811.24
Authors
Trempe, J.F.,Brown, N.R.,Noble, M.E.M.,Endicott, J.A. (deposition date: 2010-03-09, release date: 2010-03-23, Last modification date: 2024-11-20)
Primary citationTrempe, J.F.,Brown, N.R.,Noble, M.E.,Endicott, J.A.
A new crystal form of Lys48-linked diubiquitin.
Acta Crystallogr.,Sect.F, 66:994-998, 2010
Cited by
PubMed Abstract: Lys48-linked polyubiquitin chains are recognized by the proteasome as a tag for the degradation of the attached substrates. Here, a new crystal form of Lys48-linked diubiquitin (Ub2) was obtained and the crystal structure was refined to 1.6 A resolution. The structure reveals an ordered isopeptide bond in a trans configuration. All three molecules in the asymmetric unit were in the same closed conformation, in which the hydrophobic patches of both the distal and the proximal moieties interact with each other. Despite the different crystallization conditions and different crystal packing, the new crystal structure of Ub2 is similar to the previously published structure of diubiquitin, but differences are observed in the conformation of the flexible isopeptide linkage.
PubMed: 20823512
DOI: 10.1107/S1744309110027600
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.6 Å)
Structure validation

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