Literature DB >> 3026843

Structure of the porin from a bacterial stalk.

J P Chalcroft, H Engelhardt, W Baumeister.   

Abstract

The stalks (hyphae) of a prosthecate bacterium, directly sampled from the water surface of a hot pond, show extended regular patterns on their envelope in the electron microscope. Image processing revealed a structure of the crystalline complexes which is very similar to the gross morphology of the Escherichia coli porins OmpC and OmpF. The natural two-dimensional crystal of the outer membrane protein has p3 symmetry and a lattice constant of 7.95 nm. The three-dimensional structure of the stalk porin has been determined to an almost isotropic resolution of 1.7 nm. The reconstruction revealed a complex network of channels within the membrane matrix with a triplet of pores merging into a common outlet, similar to the structure of the E. coli porin OmpF in reconstituted membranes. In addition, a blindly ending pore exists which appears to be connected to the continuous pores via small channels. The significance of the regularly arrayed porin cylinders with respect to the shape and function of the stalks is discussed.

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Year:  1987        PMID: 3026843     DOI: 10.1016/0014-5793(87)81273-5

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  5 in total

Review 1.  Molecular basis of bacterial outer membrane permeability revisited.

Authors:  Hiroshi Nikaido
Journal:  Microbiol Mol Biol Rev       Date:  2003-12       Impact factor: 11.056

2.  Two-dimensional crystallization of a bacterial surface protein on lipid vesicles under controlled conditions.

Authors:  A Paul; H Engelhardt; U Jakubowski; W Baumeister
Journal:  Biophys J       Date:  1992-01       Impact factor: 4.033

3.  Nucleotide and derived amino acid sequences of the major porin of Comamonas acidovorans and comparison of porin primary structures.

Authors:  S Gerbl-Rieger; J Peters; J Kellermann; F Lottspeich; W Baumeister
Journal:  J Bacteriol       Date:  1991-04       Impact factor: 3.490

4.  The major outer membrane protein of Acidovorax delafieldii is an anion-selective porin.

Authors:  M Brunen; H Engelhardt; A Schmid; R Benz
Journal:  J Bacteriol       Date:  1991-07       Impact factor: 3.490

5.  Characterization of the porins of Campylobacter jejuni and Campylobacter coli and implications for antibiotic susceptibility.

Authors:  W J Page; G Huyer; M Huyer; E A Worobec
Journal:  Antimicrob Agents Chemother       Date:  1989-03       Impact factor: 5.191

  5 in total

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