ArticleProtein science : a publication of the Protein Society1997
Backbone makes a significant contribution to the electrostatics of alpha/beta-barrel proteins.
Article in Protein science : a publication of the Protein Society, 1997. 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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Who cites it
6 citing papers in PubMed.
- Backbone assignments and conformational dynamics in the S. typhimurium tryptophan synthase α-subunit from solution-state NMR.Journal of biomolecular NMR · 2020Article
- Structure and role for active site lid of lactate monooxygenase from Mycobacterium smegmatis.Protein science : a publication of the Protein Society · 2019Article
- Triosephosphate isomerase: a highly evolved biocatalyst.Cellular and molecular life sciences : CMLS · 2010Review
- Rapid comparison of properties on protein surface.Proteins · 2008Article
- Backbone dipoles generate positive potentials in all proteins: origins and implications of the effect.Biophysical journal · 2000Article
- Evolution of an enzyme active site: the structure of a new crystal form of muconate lactonizing enzyme compared with mandelate racemase and enolase.Proceedings of the National Academy of Sciences of the United States of America · 1998Article
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5 authors.
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Abstract
The electrostatic properties of seven alpha/beta-barrel enzymes selected from different evolutionary families were studied: triose phosphate isomerase, fructose-1,6-bisphosphate aldolase, pyruvate kinase, mandelate racemase, trimethylamine dehydrogenase, glycolate oxidase, and narbonin, a protein without any known enzymatic activity. The backbone of the alpha/beta-barrel has a distinct electrostatic field pattern, which is dipolar along the barrel axis. When the side chains are included in the calculations the general effect is to modulate the electrostatic pattern so that the electrostatic field is generally enhanced and is focused into a specific area near the active site. We use the electrostatic flux through a square surface near the active site to gauge the functionally relevant magnitude of the electrostatic field. The calculations reveal that in six out of the seven cases the backbone itself contributes greater than 45% of the total flux. The substantial electrostatic contribution of the backbone correlates with the known preference of alpha/beta-barrel enzymes for negatively charged substrates.
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