 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 2]](mh5121fig2mag.jpg)
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Figure 2
Analysis of conserved residue patterns and B-factor distribution in E. coli BamAP5. Conserved residues colour-coded in dark blue were identified on the basis of the sequence alignment shown in Supplementary Fig. S2 and subsequently mapped onto the structure. (a) The structure in orange is shown from the narrow side of the barrel. The hinge region between the BamAP5 and BamAOMP domains may allow flexible movements between these domains as indicated by arrows (left panel). The right panel depicts the same structure rotated around the y axis by 90°. (b) While there are minor interactions between BamAOMP and BamAP5 in the undisturbed structure, the third elastic network model from the elNémo analysis in blue exhibits interactions between L1/L2 and the POTRA domain. (c) The BamA structure illustrated from essentially the same orientation as in (b). Conserved residues of the structure are marked in dark blue according to the conservation pattern presented in Supplementary Fig. S2. The left panel shows a close-up of the BamAP5 and BamAOMP domain interfaces and indicates increased flexibility in turns 1 and 2 (T1 and T2) and helix 1 of BamAP5 (α1) according to the analysis of B factors (B factors are represented using rainbow colours; small B factors are marked in blue, large B factors are represented in red). The middle panel shows the conserved residues (as in Fig. 3 ![[link]](../../../../../../logos/arrows/d_arr.gif) a) of BamAP5 as well as the residues of T1 and T2 colour-coded in dark blue in the same orientation. In the right panel selected conserved residues are marked by numbers and colours (green, amphipatic residues; red, negatively charged residues; blue, positively charged residues). In BamAP5 several conserved residues are predominantly positively charged, for example Lys350, Lys361, Lys366 and Lys367, while the conserved residues in BamAOMP are mostly amphipatic. This distribution reflects the residues accounting for the interaction between FhaCOMP and FhaCP1–2, where positively charged residues in FhaCP1–2 contact hydrophilic residues in the barrel domain. (d) Analysis of conservation (left panel) and B-factor distribution (right panel) at the β1/β16 zip-like interface of BamAOMP. Residues of strands β1 and β12–β16 are particularly conserved. The majority of the β-barrel displays lower B factors and consequently a decreased mobility in comparison to the POTRA domain, turns and loop structures. |
![[Figure 2]](mh5121fig2.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
