Functional importance of a conserved sequence motif in FhaC, a prototypic member of the TpsB/Omp85 superfamily (Q27665141)

6

Françoise Jacob-Dubuisson

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Camille Locht

4

Camille Locht

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Anne-Sophie Delattre

1

Anne-Sophie Delattre

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Bernard Clantin

2

Bernard Clantin

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Nathalie Saint

3

Molecular basis of bacterial outer membrane permeability

Nathalie Saint

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language of work or name

English

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publication date

November 2010

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published in

FEBS Journal

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volume

277

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issue

22

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page(s)

4755-65

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cites work

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Conserved pore-forming regions in polypeptide-transporting proteins

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Molecular architecture and function of the Omp85 family of proteins

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Conserved Properties of Polypeptide Transport-associated (POTRA) Domains Derived from Cyanobacterial Omp85

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Role of a highly conserved bacterial protein in outer membrane protein assembly

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Functioning of outer membrane protein assembly factor Omp85 requires a single POTRA domain

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Membrane protein architects: the role of the BAM complex in outer membrane protein assembly.

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Evolutionary conservation of biogenesis of beta-barrel membrane proteins

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Machinery for protein sorting and assembly in the mitochondrial outer membrane

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The Omp85 family of proteins is essential for outer membrane biogenesis in mitochondria and bacteria.

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Membrane protein insertion: mixing eukaryotic and prokaryotic concepts

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Channel properties of TpsB transporter FhaC point to two functional domains with a C-terminal protein-conducting pore

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The crystal structure of filamentous hemagglutinin secretion domain and its implications for the two-partner secretion pathway

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The structure of the Haemophilus influenzae HMW1 pro-piece reveals a structural domain essential for bacterial two-partner secretion

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Structural and Functional Studies of Truncated Hemolysin A from Proteus mirabilis

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First structural insights into the TpsB/Omp85 superfamily.

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Two-partner secretion in Gram-negative bacteria: a thrifty, specific pathway for large virulence proteins

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Structure of the membrane protein FhaC: a member of the Omp85-TpsB transporter superfamily.

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POTRA: a conserved domain in the FtsQ family and a class of beta-barrel outer membrane proteins

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Channel formation by FhaC, the outer membrane protein involved in the secretion of the Bordetella pertussis filamentous hemagglutinin

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The evolutionarily related beta-barrel polypeptide transporters from Pisum sativum and Nostoc PCC7120 contain two distinct functional domains

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Assembly factor Omp85 recognizes its outer membrane protein substrates by a species-specific C-terminal motif

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Characterization of pores formed by YaeT (Omp85) from Escherichia coli.

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Omp85(Tt) from Thermus thermophilus HB27: an ancestral type of the Omp85 protein family

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Filling the gap, evolutionarily conserved Omp85 in plastids of chromalveolates

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Omp85 from the Thermophilic Cyanobacterium Thermosynechococcus elongatus Differs from Proteobacterial Omp85 in Structure and Domain Composition

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Amino-terminal maturation of the Bordetella pertussis filamentous haemagglutinin.

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Novel topological features of FhaC, the outer membrane transporter involved in the secretion of the Bordetella pertussis filamentous hemagglutinin

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Subtilisin-like autotransporter serves as maturation protease in a bacterial secretion pathway

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Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants

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Dissecting membrane insertion of mitochondrial beta-barrel proteins

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