The conformation of SecA, as revealed by its protease sensitivity, is altered upon interaction with ATP, presecretory proteins, everted membrane vesicles, and phospholipids.
about
Cross-talk between catalytic and regulatory elements in a DEAD motor domain is essential for SecA function.Phospholipids induce conformational changes of SecA to form membrane-specific domains: AFM structures and implication on protein-conducting channelsThe complete general secretory pathway in gram-negative bacteriaIdentification and characterization of protease-resistant SecA fragments: secA has two membrane-integral forms.Mapping of the signal peptide-binding domain of Escherichia coli SecA using Förster resonance energy transfer.Nucleotide binding induces changes in the oligomeric state and conformation of Sec A in a lipid environment: a small-angle neutron-scattering study.Comparative characterization of SecA from the alpha-subclass purple bacterium Rhodobacter capsulatus and Escherichia coli reveals differences in membrane and precursor specificity.Targeting of GroEL to SecA on the cytoplasmic membrane of Escherichia coliIcmF family protein TssM exhibits ATPase activity and energizes type VI secretion.In vivo studies of the role of SecA during protein export in Escherichia coliBoth an N-terminal 65-kDa domain and a C-terminal 30-kDa domain of SecA cycle into the membrane at SecYEG during translocationOligomeric states of the SecA and SecYEG core components of the bacterial Sec transloconFunctions of the gene products of Escherichia coli.SecD is involved in the release of translocated secretory proteins from the cytoplasmic membrane of Escherichia coli.Dissociation of the dimeric SecA ATPase during protein translocation across the bacterial membrane.OppA, the substrate-binding subunit of the oligopeptide permease, is the major Ecto-ATPase of Mycoplasma hominis.Precursor protein translocation by the Escherichia coli translocase is directed by the protonmotive force.Sites of interaction between SecA and the chaperone SecB, two proteins involved in export.
P2860
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P2860
The conformation of SecA, as revealed by its protease sensitivity, is altered upon interaction with ATP, presecretory proteins, everted membrane vesicles, and phospholipids.
description
1991 nî lūn-bûn
@nan
1991年の論文
@ja
1991年学术文章
@wuu
1991年学术文章
@zh-cn
1991年学术文章
@zh-hans
1991年学术文章
@zh-my
1991年学术文章
@zh-sg
1991年學術文章
@yue
1991年學術文章
@zh
1991年學術文章
@zh-hant
name
The conformation of SecA, as r ...... e vesicles, and phospholipids.
@en
The conformation of SecA, as r ...... e vesicles, and phospholipids.
@nl
type
label
The conformation of SecA, as r ...... e vesicles, and phospholipids.
@en
The conformation of SecA, as r ...... e vesicles, and phospholipids.
@nl
prefLabel
The conformation of SecA, as r ...... e vesicles, and phospholipids.
@en
The conformation of SecA, as r ...... e vesicles, and phospholipids.
@nl
P2093
P1476
The conformation of SecA, as r ...... ne vesicles, and phospholipids
@en
P2093
P304
P407
P577
1991-03-01T00:00:00Z