Cloning and characterization of the gene encoding for OMP-PD porin: the major Photobacterium damsela outer membrane protein.

Abstract:

:The outer membrane protein of Photobacterium damsela (OMP-PD) and the gene encoding for this porin protein were isolated and characterized. The deduced amino acid sequence of the OMP-PD monomer has 338 amino acids and a calculated molecular weight of 36,951 Da. This sequence includes a 22-amino acid signal peptide at the N-terminal, which is not found when the monomer is located in the outer membrane. Native OMP-PD protein forms a trimeric structure of approximately 110 kDa. It exhibits resistance to proteases, and it can be cleaved only following denaturation by SDS. The degree of identity of the OMP-PD amino acid sequence to porins from the Enterobacteriaceae was only 24%. Identity to Vibrio or Photobacterium porins was 38% and 48%, respectively. Nevertheless, the multiple alignment of this sequence with other structurally defined Enterobacteria porins demonstrated that the location of the 16 beta-strands and eight external loops, including a larger external L3 loop, are conserved in OMP-PD. These results, together with the previously known ability of OMP-PD to form an ion channel in artificial liposomes, strongly support its role as a porin in P. damsela and will help further investigations into the role of OMP-PD in P. damsela pathogenicity.

journal_name

Curr Microbiol

journal_title

Current microbiology

authors

Gribun A,Katcoff DJ,Hershkovits G,Pechatnikov I,Nitzan Y

doi

10.1007/s00284-003-4111-8

keywords:

subject

Has Abstract

pub_date

2004-03-01 00:00:00

pages

167-74

issue

3

eissn

0343-8651

issn

1432-0991

journal_volume

48

pub_type

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