(Q54674352)

English

Electron microscopy of thin-sectioned three-dimensional crystals of SecA protein from Escherichia coli: Structure in projection at 40 Å resolution

scientific article published on September 1, 1992

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scholarly article

1 reference

Europe PubMed Central

2 June 2018

http://europepmc.org/abstract/MED/1288619

Electron microscopy of thin-sectioned three-dimensional crystals of SecA protein from Escherichia coli: structure in projection at 40 A resolution (English)

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A1288619

9 September 2022

Electron microscopy of thin-sectioned three-dimensional crystals of SecA protein from Escherichia coli: Structure in projection at 40 Å resolution (English)

1 reference

10.1016/1047-8477(92)90040-H

https://api.crossref.org/works/10.1016/1047-8477(92)90040-H

26 November 2023

Escherichia coli proteins

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A1288619

9 September 2022

transmembrane transport protein

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A1288619

9 September 2022

Escherichia coli

1 reference

based on heuristic

inferred from title

structural biology

1 reference

10.1016/1047-8477(92)90040-H

https://api.crossref.org/works/10.1016/1047-8477(92)90040-H

26 November 2023

author name string

A. J. Weaver

1

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A1288619

9 September 2022

A. W. McDowall

2

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A1288619

9 September 2022

D. B. Oliver

3

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A1288619

9 September 2022

J. Deisenhofer

4

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A1288619

9 September 2022

language of work or name

1 reference

National Center for Biotechnology Information

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=1288619

9 September 2022

publication date

1 September 1992

1 reference

Europe PubMed Central

2 June 2018

http://europepmc.org/abstract/MED/1288619

full work available at URL

https://api.elsevier.com/content/article/PII:104784779290040H?httpAccept=text/xml

1 reference

10.1016/1047-8477(92)90040-H

https://api.crossref.org/works/10.1016/1047-8477(92)90040-H

26 November 2023

https://api.elsevier.com/content/article/PII:104784779290040H?httpAccept=text/plain

1 reference

10.1016/1047-8477(92)90040-H

https://api.crossref.org/works/10.1016/1047-8477(92)90040-H

26 November 2023

Journal of Structural Biology

1 reference

Europe PubMed Central

2 June 2018

http://europepmc.org/abstract/MED/1288619

109

1 reference

Europe PubMed Central

2 June 2018

http://europepmc.org/abstract/MED/1288619

2

1 reference

Europe PubMed Central

2 June 2018

http://europepmc.org/abstract/MED/1288619

87-96

1 reference

Europe PubMed Central

2 June 2018

http://europepmc.org/abstract/MED/1288619

SecA interacts with secretory proteins by recognizing the positive charge at the amino terminus of the signal peptide in Escherichia coli.

1

1 reference

10.1016/1047-8477(92)90040-H

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26 November 2023

SecA, an essential component of the secretory machinery of Escherichia coli, exists as homodimer.

2

1 reference

10.1016/1047-8477(92)90040-H

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Methods for specimen thickness determination in electron microscopy. II. Changes in thickness with dose

3

1 reference

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26 November 2023

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

4

1 reference

10.1016/1047-8477(92)90040-H

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26 November 2023

SecA protein is required for secretory protein translocation into E. coli membrane vesicles.

5

1 reference

10.1016/1047-8477(92)90040-H

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26 November 2023

Characterization of membrane-associated and soluble states of SecA protein from wild-type and SecA51(TS) mutant strains of Escherichia coli

6

1 reference

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Specific recognition of the leader region of precursor proteins is required for the activation of translocation ATPase of Escherichia coli

8

1 reference

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26 November 2023

Characterization of Escherichia coli SecA protein binding to a site on its mRNA involved in autoregulation.

9

1 reference

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Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein

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The binding cascade of SecB to SecA to SecY/E mediates preprotein targeting to the E. coli plasma membrane

12

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Isolation and analysis of dominant secA mutations in Escherichia coli

14

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Determination of a region in SecA that interacts with presecretory proteins in Escherichia coli.

15

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Purification of the Escherichia coli secB gene product and demonstration of its activity in an in vitro protein translocation system

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SecA protein hydrolyzes ATP and is an essential component of the protein translocation ATPase of Escherichia coli

17

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The ATPase activity of SecA is regulated by acidic phospholipids, SecY, and the leader and mature domains of precursor proteins

18

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Complementation of two overlapping fragments of SecA, a protein translocation ATPase of Escherichia coli, allows ATP binding to its amino-terminal region

19

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Solvent content of protein crystals

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Three-dimensional crystals of a membrane protein complex. The photosynthetic reaction centre from Rhodopseudomonas viridis

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SecA protein: autoregulated initiator of secretory precursor protein translocation across the E. coli plasma membrane

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Regulation of Escherichia coli secA mRNA translation by a secretion-responsive element.

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Reconstitution of translocation activity for secretory proteins from solubilized components of Escherichia coli.

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Cytosolic factor purified from Escherichia coli is necessary and sufficient for the export of a preprotein and is a homotetramer of SecB

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Purified secB protein of Escherichia coli retards folding and promotes membrane translocation of the maltose-binding protein in vitro

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Identifiers

10.1016/1047-8477(92)90040-H

1 reference

Europe PubMed Central

2 June 2018

http://europepmc.org/abstract/MED/1288619

1 reference

Europe PubMed Central

2 June 2018

http://europepmc.org/abstract/MED/1288619

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