Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Science 20 February 2004:
Vol. 303. no. 5661, pp. 1189 - 1192
DOI: 10.1126/science.1094114
Prev | Table of Contents | Next

Reports

The Structure of a Mycobacterial Outer-Membrane Channel

Michael Faller,1 Michael Niederweis,2 Georg E. Schulz1*

Mycobacteria have low-permeability outer membranes that render them resistant to most antibiotics. Hydrophilic nutrients can enter by way of transmembrane-channel proteins called porins. An x-ray analysis of the main porin from Mycobacterium smegmatis, MspA, revealed a homooctameric goblet-like conformation with a single central channel. This is the first structure of a mycobacterial outer-membrane protein. No structure-related protein was found in the Protein Data Bank. MspA contains two consecutive ß barrels with nonpolar outer surfaces that form a ribbon around the porin, which is too narrow to fit the thickness of the mycobacterial outer membrane in contemporary models.

1 Institut für Organische Chemie und Biochemie, Albert-Ludwigs-Universität, Albertstrasse 21, 79104 Freiburg im Breisgau, Germany.
2 Lehrstuhl für Mikrobiologie, Friedrich-Alexander-Universität Erlangen-Nürnberg, Staudtstrasse 5, 91058 Erlangen, Germany.

* To whom correspondence should be addressed. E-mail: schulz{at}bio.chemie.uni-freiburg.de

Read the Full Text


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Functions of the Periplasmic Loop of the Porin MspA from Mycobacterium smegmatis.
J. Huff, M. Pavlenok, S. Sukumaran, and M. Niederweis (2009)
J. Biol. Chem. 284, 10223-10231
   Abstract »    Full Text »    PDF »
Single-molecule DNA detection with an engineered MspA protein nanopore.
T. Z. Butler, M. Pavlenok, I. M. Derrington, M. Niederweis, and J. H. Gundlach (2008)
PNAS 105, 20647-20652
   Abstract »    Full Text »    PDF »
Role of Porins for Uptake of Antibiotics by Mycobacterium smegmatis.
O. Danilchanka, M. Pavlenok, and M. Niederweis (2008)
Antimicrob. Agents Chemother. 52, 3127-3134
   Abstract »    Full Text »    PDF »
Preventing Voltage-dependent Gating of Anthrax Toxin Channels Using Engineered Disulfides.
D. S. Anderson and R. O. Blaustein (2008)
J. Gen. Physiol. 132, 351-360
   Abstract »    Full Text »    PDF »
Rv1698 of Mycobacterium tuberculosis Represents a New Class of Channel-forming Outer Membrane Proteins.
A. Siroy, C. Mailaender, D. Harder, S. Koerber, F. Wolschendorf, O. Danilchanka, Y. Wang, C. Heinz, and M. Niederweis (2008)
J. Biol. Chem. 283, 17827-17837
   Abstract »    Full Text »    PDF »
Disclosure of the mycobacterial outer membrane: Cryo-electron tomography and vitreous sections reveal the lipid bilayer structure.
C. Hoffmann, A. Leis, M. Niederweis, J. M. Plitzko, and H. Engelhardt (2008)
PNAS 105, 3963-3967
   Abstract »    Full Text »    PDF »
Nutrient acquisition by mycobacteria.
M. Niederweis (2008)
Microbiology 154, 679-692
   Abstract »    Full Text »    PDF »
Designed Protein-Protein Association.
D. Grueninger, N. Treiber, M. O. P. Ziegler, J. W. A. Koetter, M.-S. Schulze, and G. E. Schulz (2008)
Science 319, 206-209
   Abstract »    Full Text »    PDF »
Corynebacterium diphtheriae: Identification and Characterization of a Channel-Forming Protein in the Cell Wall.
B. Schiffler, E. Barth, M. Daffe, and R. Benz (2007)
J. Bacteriol. 189, 7709-7719
   Abstract »    Full Text »    PDF »
The N-Terminal Domain of OmpATb Is Required for Membrane Translocation and Pore-Forming Activity in Mycobacteria.
A. Alahari, N. Saint, S. Campagna, V. Molle, G. Molle, and L. Kremer (2007)
J. Bacteriol. 189, 6351-6358
   Abstract »    Full Text »    PDF »
Porins Are Required for Uptake of Phosphates by Mycobacterium smegmatis.
F. Wolschendorf, M. Mahfoud, and M. Niederweis (2007)
J. Bacteriol. 189, 2435-2442
   Abstract »    Full Text »    PDF »
Expression of the Major Porin Gene mspA Is Regulated in Mycobacterium smegmatis.
D. Hillmann, I. Eschenbacher, A. Thiel, and M. Niederweis (2007)
J. Bacteriol. 189, 958-967
   Abstract »    Full Text »    PDF »
Topology of the Porin MspA in the Outer Membrane of Mycobacterium smegmatis.
M. Mahfoud, S. Sukumaran, P. Hulsmann, K. Grieger, and M. Niederweis (2006)
J. Biol. Chem. 281, 5908-5915
   Abstract »    Full Text »    PDF »
Structural Insights into the Secretin PulD and Its Trypsin-resistant Core.
M. Chami, I. Guilvout, M. Gregorini, H. W. Remigy, S. A. Muller, M. Valerio, A. Engel, A. P. Pugsley, and N. Bayan (2005)
J. Biol. Chem. 280, 37732-37741
   Abstract »    Full Text »    PDF »
Porins limit the intracellular persistence of Mycobacterium smegmatis.
S. Sharbati-Tehrani, J. Stephan, G. Holland, B. Appel, M. Niederweis, and A. Lewin (2005)
Microbiology 151, 2403-2410
   Abstract »    Full Text »    PDF »
PorH, a new channel-forming protein present in the cell wall of Corynebacterium efficiens and Corynebacterium callunae.
P. Hunten, B. Schiffler, F. Lottspeich, and R. Benz (2005)
Microbiology 151, 2429-2438
   Abstract »    Full Text »    PDF »
TMB-Hunt: a web server to screen sequence sets for transmembrane {beta}-barrel proteins.
A. G. Garrow, A. Agnew, and D. R. Westhead (2005)
Nucleic Acids Res. 33, W188-W192
   Abstract »    Full Text »    PDF »
Neutral Lipid Bodies in Prokaryotes: Recent Insights into Structure, Formation, and Relationship to Eukaryotic Lipid Depots.
M. Waltermann and A. Steinbuchel (2005)
J. Bacteriol. 187, 3607-3619
   Full Text »    PDF »
Multidrug Resistance of a Porin Deletion Mutant of Mycobacterium smegmatis.
J. Stephan, C. Mailaender, G. Etienne, M. Daffe, and M. Niederweis (2004)
Antimicrob. Agents Chemother. 48, 4163-4170
   Abstract »    Full Text »    PDF »
Predicting transmembrane beta-barrels in proteomes.
H. R. Bigelow, D. S. Petrey, J. Liu, D. Przybylski, and B. Rost (2004)
Nucleic Acids Res. 32, 2566-2577
   Abstract »    Full Text »    PDF »


To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)