ArticleJournal of molecular biology2010
Molecular basis for the structural stability of an enclosed β-barrel loop.
Article in Journal of molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed, 12 citations in OpenAlex.
- Type V Secretion in Gram-Negative Bacteria.EcoSal Plus · 2019Article
- Looks can be deceiving: recent insights into the mechanism of protein secretion by the autotransporter pathway.Molecular microbiology · 2015Review
- Slowing down single-molecule trafficking through a protein nanopore reveals intermediates for peptide translocation.Scientific reports · 2014Article
- Mechanistic link between β barrel assembly and the initiation of autotransporter secretion.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Molecular basis for the activation of a catalytic asparagine residue in a self-cleaving bacterial autotransporter.Journal of molecular biology · 2012Article
- Analysis of gating transitions among the three major open states of the OpdK channel.Biochemistry · 2011Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
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Abstract
We present molecular dynamics simulation studies of the structural stability of an enclosed loop in the β domain of the Escherichia coli O157:H7 autotransporter EspP. Our investigation revealed that, in addition to its excellent resistance to thermal perturbations, EspP loop 5 (L5) also has remarkable mechanical stability against pulling forces along the membrane norm. These findings are consistent with the experimental report that EspP L5 helps to maintain the permeability barrier in the outer membrane. In contrast to the major secondary structure elements of globular proteins such as ubiquitin, whose resistance to thermal and mechanical perturbations depends mainly on backbone hydrogen bonds and hydrophobic interactions, the structural stability of EspP L5 can be attributed mainly to geometric constraints and side-chain interactions dominated by hydrogen bonds. Examination of B-factors from available high-resolution structures of membrane-embedded β barrels indicates that most of the enclosed loops have stable structures. This finding suggests that loops stabilized by geometric constraints and side-chain interactions might be used more generally to restrict β-barrel channels for various functional purposes.
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Registered trials
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