Staphylococcus aureus FusB:EF-GC3 complex.

Zinc ion coordinated by FusB C-terminal domain.

A target-protection mechanism of antibiotic resistance at atomic resolution: insights into FusB-type fusidic acid resistance.

Truncation of full length EF-G to comprise domains III-V (residues 401-693).
Residues are numbered from 401 as this is a truncated form of EF-G comprising domains III-V.

This is a truncated form of the protein comprising domains III-V and beginning at residue 401
of full length EF-G. Residues 694-701 represent a non-native affinity tag.

Residues -19-0 represent a non-native affinity tag.

Truncated form of the full length EF-G protein encoded by fusA.

A structural model of the complex between the fusidic acid resistance protein FusB and a truncated form of EF-G.
This model was produced using NMR data to dock X-ray structures.

2D 1H-15N HSQC 1H R1 relaxation series (saturation recovery)

S. aureus FusB assigned chemical shifts in the apo state.

S. aureus EF-GC3 assigned chemical shifts in the apo state.

20 mM TrisHCl, 300 mM NaCl, 5 mM DTT, pH 8.0

FusB R19C mutant tagged with MTSL; 20 mM TrisHCl, 300 mM NaCl, pH 8.0

FusB T26C mutant tagged with MTSL; 20 mM TrisHCl, 300 mM NaCl, pH 8.0

FusB N150C mutant tagged with MTSL; 20 mM TrisHCl, 300 mM NaCl, pH 8.0

[U-100% 13C; U-100% 15N; partial 2H (grown in D2O with 1H glucose)]

[U-100% 15N, partial 2H (grown in D2O with 1H carbon source), 100 % natural abundance lysine]

[U-100% 15N, partial 2H (grown in D2O with 1H carbon source), 100 % natural abundance valine]

[U-100% 15N, partial 2H (grown in D2O with 1H carbon source), 100 % natural abundance phenylalanine]

[U-100% 15N, partial 2H (grown in D2O with 1H carbon source), 100 % natural abundance alanine]

[U-100% 15N, partial 2H (grown in D2O with 1H carbon source), 100 % natural abundance asparagine]

The CCPN NMR assignment and data analysis application

refinement of crystal structure to NMR parameters

Schwieters, Kuszewski, Tjandra and Clore

Department of Biochemistry, Cambridge CB2 1GA, UK

Bijvoet Center for Biomolecular Research
Padualaan 8, 3584 CH Utrecht, the Netherlands