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Review

. 2005 Mar;187(6):1879-83.

doi: 10.1128/JB.187.6.1879-1883.2005.

Vacuuming the periplasm

Olga Lomovskaya¹, Maxim Totrov

Affiliations

PMID: 15743933
PMCID: PMC1064067
DOI: 10.1128/JB.187.6.1879-1883.2005

Review

Vacuuming the periplasm

Olga Lomovskaya et al. J Bacteriol. 2005 Mar.

. 2005 Mar;187(6):1879-83.

doi: 10.1128/JB.187.6.1879-1883.2005.

Authors

Olga Lomovskaya¹, Maxim Totrov

Affiliation

¹ Mpex Pharmaceuticals, Inc., 5500 Campanile Dr., San Diego, CA 92182, USA. olomovskaya@mpexpharma.com

PMID: 15743933
PMCID: PMC1064067
DOI: 10.1128/JB.187.6.1879-1883.2005

No abstract available

PubMed Disclaimer

Figures

FIG. 1. — FIG. 1.
Cross section of AcrB. The surface of AcrB was calculated by the icmMacroShape method (M. Totrov and R. Abagyan, unpublished data) implemented as the macro in the Molsoft ICM package (MolSoft ICM 3.2 program manual; MolSoft LLC, San Diego, Calif., 2003 [http://www.molsoft.com/icm_pro.html [1]). The method generates a volume density map represented by the van der Waals potential of the molecule. Putative pathways of substrates and proton are indicated by arrows. See the text for details.

See this image and copyright information in PMC

Comment on

Aminoglycosides are captured from both periplasm and cytoplasm by the AcrD multidrug efflux transporter of Escherichia coli.
Aires JR, Nikaido H. Aires JR, et al. J Bacteriol. 2005 Mar;187(6):1923-9. doi: 10.1128/JB.187.6.1923-1929.2005. J Bacteriol. 2005. PMID: 15743938 Free PMC article.

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References

1. Abagyan, R. A., M. M. Totrov, and D. N. Kuznetsov. 1994. ICM—a new method for protein modelling and design. Applications to docking and structure prediction from the distorted native conformation. J. Comp. Chem. 15:488-506.
1. Aires, J. R., and H. Nikaido. 2005. Aminoglycosides are captured from both periplasm and cytoplasm by the AcrD multidrug efflux transporter of Escherichia coli. J. Bacteriol. 187:1923-1929. - PMC - PubMed
1. Akama, H., M. Kanemaki, M. Yoshimura, T. Tsukihara, T. Kashiwagi, H. Yoneyama, S. I. Narita, A. Nakagawa, and T. Nakae. 2004. Crystal structure of the drug-discharge outer membrane protein, OprM, of Pseudomonas aeruginosa: dual modes of membrane anchoring and occluded cavity end. J. Biol. Chem. 279:52816-52819. - PubMed
1. Akama, H., T. Matsuura, S. Kashiwagi, H. Yoneyama, S. Narita, T. Tsukihara, A. Nakagawa, and T. Nakae. 2004. Crystal structure of the membrane fusion protein, MexA, of the multidrug transporter in Pseudomonas aeruginosa. J. Biol. Chem. 279:25939-25942. - PubMed
1. Ambudkar, S. V., S. Dey, C. A. Hrycyna, M. Ramachandra, I. Pastan, and M. M. Gottesman. 1999. Biochemical, cellular, and pharmacological aspects of the multidrug transporter. Annu. Rev. Pharmacol. Toxicol. 39:361-398. - PubMed

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