Crystallographic analysis of the C-terminal domain of theEscherichia colilipoprotein BamC - Wikidata - awgldk - TriplyDB

Crystallographic analysis of the C-terminal domain of theEscherichia colilipoprotein BamC

Crystallographic analysis of the C-terminal domain of theEscherichia colilipoprotein BamC

http://www.wikidata.org/entity/Q27675721

about

The β-barrel assembly machinery in motion.Structural snapshots of the β-barrel assembly machinery.Lateral opening in the intact β-barrel assembly machinery captured by cryo-EM.Outer membrane protein biogenesis in Gram-negative bacteria 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.Lateral opening and exit pore formation are required for BamA function Dynamic association of BAM complex modules includes surface exposure of the lipoprotein BamC.The bacterial outer membrane β-barrel assembly machinery.Fitting the Pieces of the β-Barrel Assembly Machinery Complex Identification of BamC on the Surface of E. coli.Expression and Purification of the Individual Bam Components BamB-E.

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Crystallographic analysis of the C-terminal domain of theEscherichia colilipoprotein BamC

http://www.wikidata.org/entity/Q27675721

description

2011 nî lūn-bûn

@nan

2011 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի նոյեմբերին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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name

Crystallographic analysis of the C-terminal domain of theEscherichia colilipoprotein BamC

@ast

Crystallographic analysis of the C-terminal domain of theEscherichia colilipoprotein BamC

@en

Crystallographic analysis of the C-terminal domain of theEscherichia colilipoprotein BamC

@nl

type

label

Crystallographic analysis of the C-terminal domain of theEscherichia colilipoprotein BamC

@ast

Crystallographic analysis of the C-terminal domain of theEscherichia colilipoprotein BamC

@en

Crystallographic analysis of the C-terminal domain of theEscherichia colilipoprotein BamC

@nl

prefLabel

Crystallographic analysis of the C-terminal domain of theEscherichia colilipoprotein BamC

@ast

Crystallographic analysis of the C-terminal domain of theEscherichia colilipoprotein BamC

@en

Crystallographic analysis of the C-terminal domain of theEscherichia colilipoprotein BamC

@nl

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S174430911103363X

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Acta Crystallographica Section F: Structural Biology Communications

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Crystallographic analysis of the C-terminal domain of theEscherichia colilipoprotein BamC

@en

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Kelly H Kim

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

Suraaj Aulakh

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

Wendy Tan

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

P2860

Role of the AP2 beta-appendage hub in recruiting partners for clathrin-coated vesicle assembly

Membrane protein insertion: mixing eukaryotic and prokaryotic concepts.

PROCHECK: a program to check the stereochemical quality of protein structures

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

The solution structure of the outer membrane lipoprotein OmlA from Xanthomonas axonopodis pv. citri reveals a protein fold implicated in protein-protein interaction

Fold and function of polypeptide transport-associated domains responsible for delivering unfolded proteins to membranes

Crystal Structure of YaeT: Conformational Flexibility and Substrate Recognition

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

Crystal structure of Escherichia coli BamB, a lipoprotein component of the β-barrel assembly machinery complex

Structural characterization of Escherichia coli BamE, a lipoprotein component of the β-barrel assembly machinery complex

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1350-8

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scholarly article

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3250232

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10.1107/S174430911103363X

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Pt 11

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67

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P577

2011-11-01T00:00:00Z

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22102230

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condensed matter physics

structural biology

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3212449

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