Extended Data Fig. 6: Crystal structures of the BfUbb–PPIaseGS077 complex and BfUbbC70V/C76G. | Nature Microbiology

Extended Data Fig. 6: Crystal structures of the BfUbb–PPIaseGS077 complex and BfUbbC70V/C76G.

From: Bacteroides fragilis ubiquitin homologue drives intraspecies bacterial competition in the gut microbiome

Extended Data Fig. 6: Crystal structures of the BfUbb–PPIaseGS077 complex and BfUbbC70V/C76G.

a, Structural alignment of the two copies of BfUbb–PPIaseGS077 complex in one asymmetric unit. The disulfide bond formed by Cys70 and Cys76 in BfUbb and the key interacting residue Y119 in PPIaseGS077 are shown as sticks. The black arrow indicates the angle of rotation around the central axis. b, c, The binding affinities of BfUbbD75G (b) and BfUbbN7A (c) to PPIaseGS077 were measured by ITC. The N values were fixed to 1 during the data fitting. The Kd and ΔH values data are representative of 2-3 independent replicates. d, Hydrophobic interactions between R8/I44/L68/I69/C70/C76 of BfUbb (light blue) and Y56/L55/L52 of PPIaseGS077 (green). e, f, B-factor diagram of BfUbb (e) and BfUbbC70V/C76G (f) represented by the B-factor putty program in PyMOL. The cartoon thickness and color reflect the relative Cα B-factors within the molecule. The disulfide bond between C70 and C76 in BfUbb is shown as a yellow stick.

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