Skip to main content
. Author manuscript; available in PMC: 2013 Sep 5.
Published in final edited form as: Structure. 2012 Sep 5;20(9):1470–1477. doi: 10.1016/j.str.2012.08.001

Figure 3. Structure Determination of the Splice Variant HisRSΔCD by NMR Spectroscopy.

Figure 3

(A) Schematic of HisRSΔCD* (2C2S_W94Q) mutant employed for structural characterizations. The mutational sites are labeled in red and the corresponding C507, C509 and W432 residues in the native HisRS sequence are also indicated.

(B) The 1H-15N HSQC spectrum of HisRSΔCD* used for structure determination.

(C) Backbone superimposition of 20 calculated lowest-energy structures of the WHEP domain and the ABD of HisRSΔCD* are shown, and the HisRSΔCD* structure is presented below by ribbon diagram. WHEP domain (red) and ABD (green) are well folded and linked by a flexible loop.

(D) Superposition of NMR structures of HisRSΔCD* and of the WHEP domain alone (PDB: 1X59). Structures are shown in ribbon diagram. Red: WHEP domain of HisRSΔCD*, pink: 1X59.

(E) Superposition of human HisRS Δ1–53_507–509 crystal structure and HisRSΔCD* NMR structure. The W432 in HisRS FL was labeled in red. The circled area including helix α15 and the preceding loop had the most prominent differences (see also Figure S2D). Structures are shown in ribbon diagram. Orange: ABD of HisRSΔCD*, Green: ABD of HisRS FL, grey: CD of HisRS FL.

See also Table 1 and Figures S2 and S3.