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![[Figure 3]](jb5001fig3mag.jpg)
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Figure 3
Superimposition of the structure of the OmpU protomer onto three structurally analogous porin structures viewed from the extracellular side. In all cases OmpU is shown in cyan. The extracellular loops L2 and L4 and the constriction loop L3 are individually labelled. N denotes the N-terminal coil of OmpU located in the pore lumen. (a) OmpU superimposed onto protomeric OmpK36 from K. pneumoniae (magenta; PDB entry 1osm). The structures superimpose with an r.m.s.d. of 1.55 Å over 268 aligned atoms. (b) OmpU superimposed onto protomeric OmpF from E. coli (orange; PDB entry 2omf; S. W. Cowan, unpublished work). The structures superimpose with an r.m.s.d. of 1.88 Å over 217 aligned atoms. (c) OmpU superimposed onto protomeric OmpC from E. coli (red; PDB entry 2j1n; Baslé et al., 2006  ). The structures superimpose with an r.m.s.d. of 1.90 Å over 196 aligned atoms. |
![[Figure 3]](jb5001fig3.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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