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Review
. 2011:77:109-46.
doi: 10.1002/9780470920541.ch3.

Efflux pumps of the resistance-nodulation-division family: a perspective of their structure, function, and regulation in gram-negative bacteria

Mathew D Routh  1 , Yaramah Zalucki, Chih-Chia Su, Qijing Zhang, William M Shafer, Edward W Yu
Affiliations
Review

Efflux pumps of the resistance-nodulation-division family: a perspective of their structure, function, and regulation in gram-negative bacteria

Mathew D Routh et al. Adv Enzymol Relat Areas Mol Biol. 2011.
No abstract available

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Figures

Figure 1
Figure 1
Model of the assembled tripartite drug efflux pump of AcrAB-TolC in the form of TolC3-AcrA3-AcrB3. This possible model is generated based on the crystal structures of individual components of the complex in addition to cross-linked data between AcrA, AcrB, and TolC. The TolC trimer [orange, red, and yellow subunits with gray equatorial domains and outer membrane (OM) regions] was docked onto AcrA (green)-docked AcrB trimer (blue/light blue subunits with gray inner membrane (IM) regions). [From (45), with permission from the National Academy of Sciences and V. Koronakis.] (See insert for color representation.)
Figure 2
Figure 2
Structural comparison of the P31 and P2221 structures of AcrR. Superimposition of the dimeric AcrR structures was performed using the program ESCET (green, P31 structure; orange, P2221 structure). The conformational differences highlighted in these two crystal structures provide a plausible model to describe transcriptional regulation by AcrR. Residue E67 in each subunit is shown as a stick model. (See insert for color representation.)
Figure 3
Figure 3
Crystal structure of the CusB membrane fusion protein. The structure can be divided into four distinct domains. Domain 1 is formed by the N- and C-termini and is located above the inner membrane. The loops between domains 2 and 3 appear to form an effective hinge to allow the molecule to shift from an open conformation to a more compact structure. Domain 4 is folded into an antiparallel, three-helix bundle, which is thought to be located near the outer membrane. (See insert for color representation.)
Figure 4
Figure 4
Specific interaction between CusA and CusB. The model of CusA (gray) was created based on protein sequence alignment and the crystal structure of AcrB. Mass spectral data suggest that the periplasmic domain of CusA specifically interacts with the N-terminus of CusB (light brown). Polypeptides α, SGKHDLADLR (from CusA), and β, IDPTQTQNLGVKTATVTR (from CusB), are shown in red and blue, respectively. (See insert for color representation.)
Figure 5
Figure 5
Crystal structure of the CmeR regulator. The dimeric structure of CmeR indicates that CmeR is an all-helical protein (α1-α10 and α1'-α10', respectively) which can easily be divided into two domains (the N-terminal DNA-binding and C-terminal ligand-binding domains). The bound glycerol molecule in each subunit of CmeR is represented as a hard-sphere model. (See insert for color representation.)
Figure 6
Figure 6
Proposed model of the regulatory system in N. gonorrhoeae. Shown is a proposed regulatory system in N. gonorrhoeae strain FA19 that impacts levels of antimicrobial resistance via drug efflux pumps. The lines with bars indicate transcriptional repression; the lines with arrows indicate transcriptional activation.
See this image and copyright information in PMC

References

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