Crystal structure of the ubiquitin-like protein YukD from Bacillus subtilis.
The YukD protein in Bacillus subtilis was identified in a hidden Markov model (HMM) search as being related in sequence to ubiquitin. By solving the crystal structure we show that YukD adopts a fold that is most closely related to ubiquitin, yet has the shortest C-terminal tail of all known ubiquitin-like proteins. The endogenous gene of yukD in B. subtilis was disrupted without an obvious phenotypic effect and an inducible copy encoding a C-Myc and His-tagged version of the protein was introduced at the ectopic locus amyE. Conjugation assays performed both in vitro and in vivo indicate that YukD lacks the capacity for covalent bond formation with other proteins.
van den Ent
Fusinita
F
MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK. fent@mrc-lmb.cam.ac.uk
Löwe
Jan
J
D000595:Amino Acid Sequence; D001412:Bacillus subtilis / Q000235:genetics / Q000378:metabolism*; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D003460:Crystallization; D003461:Crystallography; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D014452:Ubiquitins / Q000737:chemistry* / Q000235:genetics
D001426:Bacterial Proteins; D014452:Ubiquitins