Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

A large conformational change couples the ATP binding site of SecA to the SecY protein channel.

Journal of molecular biology - 7 Dec 2007

Robson Alice, Booth Antonia E G, Gold Vicki A M, Clarke Anthony R, Collinson Ian

Abstract excerpt

In bacteria, the SecYEG protein translocation complex employs the cytosolic ATPase SecA to couple the energy of ATP binding and hydrolysis to the mechanical force required to push polypeptides through the membrane. The molecular basis of this energy transducing reaction is not well understood. A peptide-binding array has been employed to identify sites on SecYEG that interact with SecA. These results along with...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Adenosine Triphosphatases
Share to Adenosine Triphosphate

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Cations, Divalent

Share to Dimerization

Share to Magnesium

Share to Membrane Transport Proteins

Share to SEC Translocation Channels

Share to SecA Proteins

Source

Identifiers

PMID: 17964601
DOI: 10.1016/j.jmb.2007.09.086

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A large conformational change couples the ATP binding site of SecA to the SecY protein channel.PMID 17964601Read ↗

SecA membrane cycling at SecYEG is driven by distinct ATP binding and hydrolysis events and is regulated by SecD and SecF.Semantic proximity Read ↗

Quaternary dynamics of the SecA motor drive translocase catalysis.Semantic proximity Read ↗

Dynamic action of the Sec machinery during initiation, protein translocation and termination.Semantic proximity Read ↗

In vivo membrane topology of Escherichia coli SecA ATPase reveals extensive periplasmic exposure of multiple functionally important domains clustering on one face of SecA.Semantic proximity Read ↗

Unlocking the Bacterial SecY Translocon.Semantic proximity Read ↗

Nucleotide exchange from the high-affinity ATP-binding site in SecA is the rate-limiting step in the ATPase cycle of the soluble enzyme and occurs through a specialized conformational state.Semantic proximity Read ↗

Translocation of proteins through the Sec61 and SecYEG channels.Semantic proximity Read ↗

Roles of SecG in ATP- and SecA-dependent protein translocation.Semantic proximity Read ↗

Mechanism of conformational coupling in SecA: Key role of hydrogen-bonding networks and water interactions.Semantic proximity Read ↗

SecY and SecA interact to allow SecA insertion and protein translocation across the Escherichia coli plasma membrane.Semantic proximity Read ↗

Functionally significant mobile regions of Escherichia coli SecA ATPase identified by NMR.Semantic proximity Read ↗

Identification of the magnesium-binding domain of the high-affinity ATP-binding site of the Bacillus subtilis and Escherichia coli SecA protein.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.