 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 5]](mn5088fig5mag.jpg)
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Figure 5
(a) Overview of the 2.95 Å resolution crystal structure of ctMex67LRR-NTF2L. Two copies of the protein in the asymmetric unit were assumed in a homodimeric configuration analogous to that of S. cerevisiae NTF2 (Bayliss et al., 2002  ; PDB entry 1gyb). Residues corresponding to the LRR-NTF2L linker (residues 362–378) were disordered as depicted in the schematic representation using dotted lines. (b) Structural alignment of the two copies of ctMex67LRR-NTF2L in the asymmetric unit; the LRR domain was placed in the same position with respect to the NTF2L domain in both copies. A Cα r.m.s.d. of 1.03 Å was observed over 294 residues. (c) Schematic of the secondary-structure elements present in the NTF2L domain for the structure of ctMex67LRR-NTF2L. No major changes in the NTF2-like core were observed, although rearrangements in the loop regions were detected. The pre-α1 loop which was previously ordered in the structure of ctMex67NTF2L–Mtr2 was disordered in this structure (depicted as a dotted red line). (d) View of the electrostatic surface potential of the β-sheet interface between the two NTF2L domains. The `NXF plug' previously identified to confer specificity for the Mex67–Mtr2 interaction (Kerkow et al., 2012) was still present in this structure of homodimeric Mex67. (e) Three representative views of the final 2Fo − Fc maps for the ctMex67LRR-NTF2L structure contoured at the 1σ level (one copy of ctMex67LRR-NTF2L is shown in yellow and the other is shown in green). |
![[Figure 5]](mn5088fig5.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
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