view article

Figure 1
Crystal structure of Lys48-linked Ub2. (a) Cartoon representation of a Ub2 molecule in the crystal structure. The proximal and distal moieties are coloured magenta and cyan, respectively. The atoms forming the isopeptide bond as well as the interface residues Ile44 and Val70 are shown as sticks. Residues labelled with primes belong to the distal moiety. (b) Close-up view of the residues forming the interface between the distal and proximal subunits. The molecular surface of the proximal subunit is displayed in transparent white. (c) Cross-eye stereoview ribbon display of the overlaid Ub2 crystal structures. The three chains in the new crystal structure are shaded yellow, blue and red for ABCD and EF, respectively. The previously reported crystal structure of Ub2 is shaded in magenta (PDB code 1aar; Cook et al., 1992BB3). Residues that have different conformations in different subunits are labelled. The disordered C-termini of the proximal moieties are labelled `C'.

ISSN: 2053-230X
Follow Acta Cryst. F
Sign up for e-alerts
Follow Acta Cryst. on Twitter
Follow us on facebook
Sign up for RSS feeds