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Crystal structure of the ubiquitin‐like protein YukD from Bacillus subtilis
Author(s) -
van den Ent Fusinita,
Löwe Jan
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.06.002
Subject(s) - bacillus subtilis , ubiquitin , gene , biology , in vitro , genetics , biochemistry , chemistry , microbiology and biotechnology , computational biology , bacteria
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.