 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 1]](wd5258fig1mag.jpg)
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Figure 1
Design of an hsAar2 loop-truncation mutant based on sequence alignment and structural comparison employing a homology model derived from HHpred. (a) The alignment of the human and yeast Aar2 sequences was prepared by ClustalX2 (Larkin et al., 2007  ) and shaded with ALSCRIPT (Barton, 1993). Conservation is indicated by a grey background and identity by a black background. The numbering above the alignment refers to human Aar2. Below the alignment, secondary-structure elements of yeast Aar2 as detected with PROMOTIF (Hutchinson & Thornton, 1996) in the yeast Aar2Δloop–RH–JM complex structure are shown in red. Boxed residues indicate residues that were replaced by three or five serines in human and yeast Aar2Δloop, respectively. Blue triangles above the alignment indicate residues of yeast Aar2Δloop in contact with yeast RH. (b) Superimposition of yeast Aar2 (PDB entry 3sbt
; Weber et al., 2011) and a homology model of human Aar2 derived from HHpred based on the yeast Aar2p structure (Söding et al., 2005). The inset shows a close-up view of the flexible internal hsAar2 loop which was replaced by three serine residues (3S) bridging residues Arg201 and His169 in hsAar2Δloop. |
![[Figure 1]](wd5258fig1.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
