Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
A FAMILY OF GRAM-NEGATIVE BACTERIAL OUTER-MEMBRANE FACTORS THAT FUNCTION IN THE EXPORT OF PROTEINS, CARBOHYDRATES, DRUGS AND HEAVY-METALS FROM GRAM-NEGATIVE BACTERIA
Autore:
PAULSEN IT; PARK JH; CHOI PS; SAIER MH;
Indirizzi:
UNIV CALIF SAN DIEGO,DEPT BIOL LA JOLLA CA 92093 UNIV CALIF SAN DIEGO,DEPT BIOL LA JOLLA CA 92093
Titolo Testata:
FEMS microbiology letters
fascicolo: 1, volume: 156, anno: 1997,
pagine: 1 - 8
SICI:
0378-1097(1997)156:1<1:AFOGBO>2.0.ZU;2-K
Fonte:
ISI
Lingua:
ENG
Soggetto:
ESCHERICHIA-COLI; EFFLUX; TRANSPORT; SECRETION; RESISTANCE; RESOLUTION; SEQUENCES; ALIGNMENT; PUMPS; PORIN;
Keywords:
TRANSPORT; OUTER MEMBRANE; BETA-BARREL; GRAM-NEGATIVE BACTERIA; ACTIVE EXPORT; PROTEIN; COMPLEX CARBOHYDRATE; DRUG; HEAVY METAL;
Tipo documento:
Review
Natura:
Periodico
Citazioni:
28
Recensione:
Indirizzi per estratti:
Citazione:
I.T. Paulsen et al., "A FAMILY OF GRAM-NEGATIVE BACTERIAL OUTER-MEMBRANE FACTORS THAT FUNCTION IN THE EXPORT OF PROTEINS, CARBOHYDRATES, DRUGS AND HEAVY-METALS FROM GRAM-NEGATIVE BACTERIA", FEMS microbiology letters, 156(1), 1997, pp. 1-8

Abstract

Gram-negative bacteria have evolved transport complexes that export macromolecules and toxic substances across the two membranes of the cell envelope in a single energy coupled step. The process requires (1) acytoplasmic membrane export system, (2) a membrane fusion protein (MFP), and (3) an outer membrane factor (OMF). Families comprising the former two constituents have been described previously. We here present an analysis of the phylogenetic and structural characteristics of the OMF family. Twenty-one members of this family have been identified, and based on available evidence, they function in conjunction with ABC, RND, MFS and/or other types of cytoplasmic transport systems. OMFs exhibit fairly uniform sizes (398-495 residues with two exceptions), and based on computational analyses, they may form beta-barrel structures consisting of up to 16 beta-strands. Phylogenetic analyses reveal thatwhile the MFPs cluster in accordance with the type of cytoplasmic membrane transport systems with which they function, OMFs do not. We conclude that OMFs probably comprise a family of outer membrane porin-typeproteins of uniform structure which did not coevolve with their cognate cytoplasmic membrane transport systems.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/11/20 alle ore 06:59:57