Three-dimensional structure of the bacterial protein-translocation complex SecYEG (Q28217206)

3

object named as

Tom A Rapoport

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Ian Collinson

object named as

Ian Collinson

5

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author name string

Cécile Breyton

1

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Winfried Haase

A mammalian homolog of SEC61p and SECYp is associated with ribosomes and nascent polypeptides during translocation

2

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language of work or name

Englisch

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publication date

8 August 2002

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published in

Nature

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volume

418

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issue

6898

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page(s)

662-5

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cites work

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The purified E. coli integral membrane protein SecY/E is sufficient for reconstitution of SecA-dependent precursor protein translocation.

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Reconstitution of a protein translocation system containing purified SecY, SecE, and SecA from Escherichia coli

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Oligomeric Rings of the Sec61p Complex Induced by Ligands Required for Protein Translocation

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The Structure of Ribosome-Channel Complexes Engaged in Protein Translocation

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Architecture of the protein-conducting channel associated with the translating 80S ribosome

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SecYEG assembles into a tetramer to form the active protein translocation channel

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Projection structure and oligomeric properties of a bacterial core protein translocase

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Distinct catalytic roles of the SecYE, SecG and SecDFyajC subunits of preprotein translocase holoenzyme

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The SecYEG preprotein translocation channel is a conformationally dynamic and dimeric structure

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Signal sequence recognition in posttranslational protein transport across the yeast ER membrane.

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Mapping the sites of interaction between SecY and SecE by cysteine scanning mutagenesis.

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SecA promotes preprotein translocation by undergoing ATP-driven cycles of membrane insertion and deinsertion.

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The catalytic cycle of the escherichia coli SecA ATPase comprises two distinct preprotein translocation events

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The protease-protected 30 kDa domain of SecA is largely inaccessible to the membrane lipid phase

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Escherichia coli SecA shape and dimensions

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SDS-digested freeze-fracture replica labeling electron microscopy to study the two-dimensional distribution of integral membrane proteins and phospholipids in biomembranes: practical procedure, interpretation and application

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Assessment of electron crystallographic data obtained from two-dimensional crystals of biological specimens

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Inversion of the membrane topology of SecG coupled with SecA-dependent preprotein translocation

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7 January 2021

Topology analysis of the SecY protein, an integral membrane protein involved in protein export in Escherichia coli.

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Disruption of the gene encoding p12 (SecG) reveals the direct involvement and important function of SecG in the protein translocation of Escherichia coli at low temperature.

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Cysteine-Directed Cross-Linking Demonstrates That Helix 3 of SecE Is Close to Helix 2 of SecY and Helix 3 of a Neighboring SecE†

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Use of antibody fragments (Fv) in immunocytochemistry

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