The bacterial porin superfamily: sequence alignment and structure prediction.

Abstract:

:The porins of Gram-negative bacteria are responsible for the 'molecular sieve' properties of the outer membrane. They form large water-filled channels which allow the diffusion of hydrophilic molecules into the periplasmic space. Owing to the strong hydrophilicity of their amino acid sequence and the nature of their secondary structure (beta strands), conventional hydropathy methods for predicting membrane topology are useless for this class of protein. The large number of available porin amino acid sequences was exploited to improve the accuracy of the prediction in combination with tools detecting amphipathicity of secondary structure. Using the constraints of beta-sheet structure these porins are predicted to contain 16 membrane-spanning strands, 14 of which are common to the two (enteric and the neisserial) porin subfamilies.

journal_name

Mol Microbiol

journal_title

Molecular microbiology

authors

Jeanteur D,Lakey JH,Pattus F

doi

10.1111/j.1365-2958.1991.tb02145.x

subject

Has Abstract

pub_date

1991-09-01 00:00:00

pages

2153-64

issue

9

eissn

0950-382X

issn

1365-2958

journal_volume

5

pub_type

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