 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 1]](nw5136fig1_combined_mag.jpg)
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Figure 1
The overall structure of Endo HSα. (a) Overall structure of Endo HSα shown in two orientations. The left panel displays a top-down view along the axis of the TIM barrel, which corresponds to domain I. The right panel shows a side view obtained by rotating the structure 90° around the x axis. Individual domains are color-coded as follows: domain I, green; domain II, blue; domain III, red; domain IV, cyan; domain V, pink. Two long loops connecting domain IV are highlighted, with the N-terminal side shown in orange and the C-terminal side in yellow. (b) Structural superposition of Endo A (PDB entry 3fha, red) and Endo D (PDB entry 2w92, purple) onto Endo HSα (green), based on domains I to III. This view is rotated 180° around the x axis from the right panel of (a). The regions with different numbers of β-strands among the three structures are highlighted in a dark color to emphasize the structural variation. (c) Topology diagrams of domains II and III. In domain II the additional β-strand observed in Endo A is indicated with a black dotted arrow, whereas the β-strand conserved in Endo A and Endo HSα but absent in Endo D is indicated with a red arrow. In domain III of Endo HSα, the β-strand formed by the region between domains IV and V is shown with a red arrow. (d) Close-up view of the domain interface between domain IV and adjacent domains. The residues involved in the interdomain interactions are highlighted. Domain colors are consistent with those shown in (a). |
![[Figure 1]](nw5136fig1_combined.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
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