 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 3]](hc5199fig3mag.jpg)
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Figure 3
Alignment of monomeric, closed SapA structures. (a) Sequence diagram of human SapA. The highlighted features are cysteines that form disulfide bonds (yellow circles) and asparagines where N-linked glycosylation occurs (pink diamonds). The bar graphs beneath the sequence show the backbone r.m.s.d. per residue after least-squares fit alignment of PDB entry 2dob with chain A, of PDB entry 2dob with chain B and of chain A with chain B. Dark grey bars indicate r.m.s.d > 1.0 Å. (b) Least-squares fit alignment of the human SapA structure determined here (chain A, purple; chain B, teal) with the previous structure at pH 6.0 (PDB entry 2dob, grey). Ribbon thickness in nonhelical regions is proportional to atomic B factor. Details of the greatest conformational differences are shown as sticks, including flexible hinge coil regions (indicated) and the outer surface of the α2 helix. |
![[Figure 3]](hc5199fig3.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
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