PDBsum entry 1yc9

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Membrane protein PDB id
Protein chain
411 a.a.
_HG ×2
Waters ×315

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Key reference
Title The crystal structure of the outer membrane protein vcec from the bacterial pathogen vibrio cholerae at 1.8 a resolution.
Authors L.Federici, D.Du, F.Walas, H.Matsumura, J.Fernandez-Recio, K.S.Mckeegan, M.I.Borges-Walmsley, B.F.Luisi, A.R.Walmsley.
Ref. J Biol Chem, 2005, 280, 15307-15314. [DOI no: 10.1074/jbc.M500401200]
PubMed id 15684414
Multidrug resistance in Gram-negative bacteria arises in part from the activities of tripartite drug efflux pumps. In the pathogen Vibrio cholerae, one such pump comprises the inner membrane proton antiporter VceB, the periplasmic adaptor VceA, and the outer membrane channel VceC. Here, we report the crystal structure of VceC at 1.8 A resolution. The trimeric VceC is organized in the crystal lattice within laminar arrays that resemble membranes. A well resolved detergent molecule within this array interacts with the transmembrane beta-barrel domain in a fashion that may mimic protein-lipopolysaccharide contacts. Our analyses of the external surfaces of VceC and other channel proteins suggest that different classes of efflux pumps have distinct architectures. We discuss the implications of these findings for mechanisms of drug and protein export.
Figure 4.
FIG. 4. Electrostatic charge distribution of VceC, TolC, and OprM. For clarity, one protomer was removed to show the channel interior. Red indicates electronegativity, blue electropositivity, and white represents neutrality.
Figure 5.
FIG. 5. Proposed opening mechanism for the VceC channel. a, superimposition of the closed and open states. The moving helices H7 and H8 of one protomer are highlighted in purple (closed state) and magenta (open state). b, polar interactions between protomers that stabilize the closed state. c, polar interactions within the same protomer that stabilize the closed state.
The above figures are reprinted by permission from the ASBMB: J Biol Chem (2005, 280, 15307-15314) copyright 2005.
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