ArticleActa crystallographica. Section F, Structural biology and crystallization communications2009
Structure of the twin-arginine signal-binding protein DmsD from Escherichia coli.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
11 citing papers in PubMed, 19 citations in OpenAlex.
- History of Maturation of Prokaryotic Molybdoenzymes-A Personal View.Molecules (Basel, Switzerland) · 2023Review
- Highly Active Small Aminated Quinolinequinones against Drug-ResistantMolecules (Basel, Switzerland) · 2022Article
- Analysis of haloarchaeal twin-arginine translocase pathway reveals the diversity of the machineries.Heliyon · 2019Article
- 1,4-Naphthoquinone Analogues: Potent Antibacterial Agents and Mode of Action Evaluation.Molecules (Basel, Switzerland) · 2019Article
- Evaluating a New High-throughput Twin-Arginine Translocase Assay in Bacteria for Therapeutic Applications.Current microbiology · 2017Article
- Biosynthesis of selenate reductase in Salmonella enterica: critical roles for the signal peptide and DmsD.Microbiology (Reading, England) · 2016Article
- Biosynthesis and Insertion of the Molybdenum Cofactor.EcoSal Plus · 2015Review
- Unique Photobleaching Phenomena of the Twin-Arginine Translocase Respiratory Enzyme Chaperone DmsD.The open biochemistry journal · 2014Article
- The hydrophobic region of the DmsA twin-arginine leader peptide determines specificity with chaperone DmsD.Biochemistry · 2013Article
- Characterization of a pre-export enzyme-chaperone complex on the twin-arginine transport pathway.The Biochemical journal · 2013Article
- Conformational selection underlies recognition of a molybdoenzyme by its dedicated chaperone.PloS one · 2012Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The translocation of folded proteins via the twin-arginine translocation (Tat) pathway is regulated to prevent the futile export of inactive substrate. DmsD is part of a class of cytoplasmic chaperones that play a role in preventing certain redox proteins from premature transport. DmsD from Escherichia coli has been crystallized in space group P4(1)2(1)2, with unit-cell parameters a = b = 97.45, c = 210.04 A, in the presence of a small peptide. The structure has been solved by molecular replacement to a resolution of 2.4 A and refined to an R factor of 19.4%. There are four molecules in the asymmetric unit that may mimic a higher order structure in vivo. There appears to be density for the peptide in a predicted binding pocket, which lends support to its role as the signal-recognition surface for this class of proteins.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.