ArticleProtein science : a publication of the Protein Society2012
Formyl-coenzyme A (CoA):oxalate CoA-transferase from the acidophile Acetobacter aceti has a distinctive electrostatic surface and inherent acid stability.
Article in Protein science : a publication of the Protein Society, 2012. 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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Who cites it
11 citing papers in PubMed, 20 citations in OpenAlex.
- Polyextremophile engineering: a review of organisms that push the limits of life.Frontiers in microbiology · 2024Review
- Structural Basis for a Cork-Up Mechanism of the Intra-Molecular Mesaconyl-CoA Transferase.Biochemistry · 2023Article
- Redefining the coenzyme A transferase superfamily with a large set of manually annotated proteins.Protein science : a publication of the Protein Society · 2022Article
- Crystal Structure of an Intramolecular Mesaconyl-Coenzyme A Transferase From the 3-Hydroxypropionic Acid Cycle ofFrontiers in microbiology · 2022Article
- Leucine-Responsive Regulatory Protein in Acetic Acid Bacteria Is Stable and Functions at a Wide Range of Intracellular pH Levels.Journal of bacteriology · 2021Article
- Review
- Biofilm Mode of Cultivation Leads to an Improvement of the Entomotoxic Patterns of TwoMicroorganisms · 2020Article
- Structural characterization of HypX responsible for CO biosynthesis in the maturation of NiFe-hydrogenase.Communications biology · 2019Article
- Effect of Sequential Acclimation to Various Carbon Sources on the Proteome ofFrontiers in microbiology · 2019Article
- Structure-based functional annotation of hypothetical proteins from Candida dubliniensis: a quest for potential drug targets.3 Biotech · 2015Article
- Article
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Authors and funding
6 authors at 2 institutions in 1 country.
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Abstract
Bacterial formyl-CoA:oxalate CoA-transferase (FCOCT) and oxalyl-CoA decarboxylase work in tandem to perform a proton-consuming decarboxylation that has been suggested to have a role in generalized acid resistance. FCOCT is the product of uctB in the acidophilic acetic acid bacterium Acetobacter aceti. As expected for an acid-resistance factor, UctB remains folded at the low pH values encountered in the A. aceti cytoplasm. A comparison of crystal structures of FCOCTs and related proteins revealed few features in UctB that would distinguish it from nonacidophilic proteins and thereby account for its acid stability properties, other than a strikingly featureless electrostatic surface. The apparently neutral surface is a result of a "speckled" charge decoration, in which charged surface residues are surrounded by compensating charges but do not form salt bridges. A quantitative comparison among orthologs identified a pattern of residue substitution in UctB that may be a consequence of selection for protein stability by constant exposure to acetic acid. We suggest that this surface charge pattern, which is a distinctive feature of A. aceti proteins, creates a stabilizing electrostatic network without stiffening the protein or compromising protein-solvent interactions.
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