(Q54499897)

30 May 2018

title

Structure of the periplasmic chaperone Skp suggests functional similarity with cytosolic chaperones despite differing architecture. (English)

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30 May 2018

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3

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author name string

Ingo P Korndörfer

series ordinal

1

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30 May 2018

Monica K Dommel

series ordinal

2

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publication date

12 September 2004

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30 May 2018

Nature Structural & Molecular Biology

published in

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30 May 2018

volume

11

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issue

10

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30 May 2018

page(s)

1015-1020

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30 May 2018

https://scigraph.springernature.com/pub.10.1038/nsmb828

exact match

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cites work

Skp is a periplasmic Escherichia coli protein requiring SecA and SecY for export

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A periplasmic protein (Skp) of Escherichia coli selectively binds a class of outer membrane proteins.

21 January 2018

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The early interaction of the outer membrane protein phoe with the periplasmic chaperone Skp occurs at the cytoplasmic membrane

21 January 2018

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Structure of the outer membrane protein A transmembrane domain

21 January 2018

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Crystal structures explain functional properties of two E. coli porins

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Crystal structures of various maltooligosaccharides bound to maltoporin reveal a specific sugar translocation pathway

21 January 2018

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Folding and insertion of the outer membrane protein OmpA is assisted by the chaperone Skp and by lipopolysaccharide

21 January 2018

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

21 January 2018

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The periplasmic E. coli chaperone Skp is a trimer in solution: biophysical and preliminary crystallographic characterization

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Structure of eukaryotic prefoldin and of its complexes with unfolded actin and the cytosolic chaperonin CCT.

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The crystal structure of the peptide-binding fragment from the yeast Hsp40 protein Sis1

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The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex

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Structure and biogenesis of the capsular F1 antigen from Yersinia pestis: preserved folding energy drives fiber formation

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Lipocalins as a scaffold

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Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin

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Targeting and assembly of periplasmic and outer-membrane proteins in Escherichia coli

21 January 2018

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Skp, a molecular chaperone of gram-negative bacteria, is required for the formation of soluble periplasmic intermediates of outer membrane proteins

31 March 2020

1 reference

Affinity of the periplasmic chaperone Skp of Escherichia coli for phospholipids, lipopolysaccharides and non-native outer membrane proteins. Role of Skp in the biogenesis of outer membrane protein

31 March 2020

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Calculating Partition Coefficients of Peptides by the Addition Method

31 March 2020

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31 March 2020

Identifiers

DOI

10.1038/NSMB828

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30 May 2018

PubMed ID

15361861

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30 May 2018