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The structural basis of autotransporter translocation by TamA

The structural basis of autotransporter translocation by TamA

http://www.wikidata.org/entity/Q27686750

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Structure of BamA, an essential factor in outer membrane protein biogenesis Structure of the BAM complex and its implications for biogenesis of outer-membrane proteins Extreme Dynamics in the BamA β-Barrel Seam.The POTRA domains of Toc75 exhibit chaperone-like function to facilitate import into chloroplasts.The β-barrel assembly machinery in motion.Lateral opening in the intact β-barrel assembly machinery captured by cryo-EM.The TamB ortholog of Borrelia burgdorferi interacts with the β-barrel assembly machine (BAM) complex protein BamA From Chaperones to the Membrane with a BAM!How does a β-barrel integral membrane protein insert into the membrane?Impact of holdase chaperones Skp and SurA on the folding of β-barrel outer-membrane proteins.A combined kinetic push and thermodynamic pull as driving forces for outer membrane protein sorting and folding in bacteria.Dynamic interplay of membrane-proximal POTRA domain and conserved loop L6 in Omp85 transporter FhaC.Conserved Omp85 lid-lock structure and substrate recognition in FhaC Assembly of the secretion pores GspD, Wza and CsgG into bacterial outer membranes does not require the Omp85 proteins BamA or TamA.Looks can be deceiving: recent insights into the mechanism of protein secretion by the autotransporter pathway.The β-barrel membrane protein insertase machinery from Gram-negative bacteria.Characterization of the insertase BamA in three different membrane mimetics by solution NMR spectroscopy.Insight into the conformational stability of membrane-embedded BamA using a combined solution and solid-state NMR approach.TtOmp85, a β-barrel assembly protein, functions by barrel augmentation Versatile in vitro system to study translocation and functional integration of bacterial outer membrane proteins.Evolution and targeting of Omp85 homologs in the chloroplast outer envelope membrane.Translocation path of a substrate protein through its Omp85 transporter.A comprehensive analysis of the Omp85/TpsB protein superfamily structural diversity, taxonomic occurrence, and evolution.Lateral opening and exit pore formation are required for BamA function Conformational dynamics of protein transporter FhaC: large-scale motions of plug helix.Lateral gates: β-barrels get in on the act.Two-Partner Secretion: Combining Efficiency and Simplicity in the Secretion of Large Proteins for Bacteria-Host and Bacteria-Bacteria Interactions Multiple driving forces required for efficient secretion of autotransporter virulence proteins DegP Chaperone Suppresses Toxic Inner Membrane Translocation Intermediates.Fitting the Pieces of the β-Barrel Assembly Machinery Complex Reconstitution of a nanomachine driving the assembly of proteins into bacterial outer membranes.Dynamics and Energy Contributions for Transport of Unfolded Pertactin through a Protein Nanopore.Structural Basis for Translocation of a Biofilm-supporting Exopolysaccharide across the Bacterial Outer Membrane.Mechanistic studies of the biogenesis and folding of outer membrane proteins in vitro and in vivo: what have we learned to date?The β-Barrel Assembly Machinery Complex.Crystallization of Membrane Proteins: An Overview.Protein folding in the cell envelope of Escherichia coli.Structural basis for substrate selection by the translocation and assembly module of the β-barrel assembly machinery.Conserved features in TamA enable interaction with TamB to drive the activity of the translocation and assembly module Microseed matrix screening for optimization in protein crystallization: what have we learned?

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The structural basis of autotransporter translocation by TamA

http://www.wikidata.org/entity/Q27686750

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2013 nî lūn-bûn

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2013 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

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2013 թվականի նոյեմբերին հրատարակված գիտական հոդված

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2013年の論文

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The structural basis of autotransporter translocation by TamA

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The structural basis of autotransporter translocation by TamA

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The structural basis of autotransporter translocation by TamA

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The structural basis of autotransporter translocation by TamA

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The structural basis of autotransporter translocation by TamA

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The structural basis of autotransporter translocation by TamA

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The structural basis of autotransporter translocation by TamA

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The structural basis of autotransporter translocation by TamA

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P2093

Fabian Gruss

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Franziska Zähringer

http://www.w3.org/2001/XMLSchema#string

Timm Maier

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P2860

Structure and function of an essential component of the outer membrane protein assembly machine

Crystal structure of a full-length autotransporter

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

Structure and Flexibility of the Complete Periplasmic Domain of BamA: The Protein Insertion Machine of the Outer Membrane

Coot: model-building tools for molecular graphics

Experimental phasing with SHELXC/D/E: combining chain tracing with density modification

Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega

Phasercrystallographic software

Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7

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