ArticleProceedings of the National Academy of Sciences of the United States of America2016
Disorder drives cooperative folding in a multidomain protein.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Determinants of Protein Folding Pathways: Lessons from Metamorphic Proteins.International journal of molecular sciences · 2026Review
- A PDZ tandem repeat folds and unfolds via different pathways.Protein science : a publication of the Protein Society · 2024Article
- Polymicrobial interactions betweenbioRxiv : the preprint server for biology · 2024Article
- Folding and Binding Kinetics of the Tandem of SH2 Domains from SHP2.International journal of molecular sciences · 2024Article
- On the Effects of Disordered Tails, Supertertiary Structure and Quinary Interactions on the Folding and Function of Protein Domains.Biomolecules · 2022Review
- Deep learning in prediction of intrinsic disorder in proteins.Computational and structural biotechnology journal · 2022Review
- First Principles Calculation of Protein-Protein Dimer Affinities of ALS-Associated SOD1 Mutants.Frontiers in molecular biosciences · 2022Article
- Hidden kinetic traps in multidomain folding highlight the presence of a misfolded but functionally competent intermediate.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- The streptococcal multidomain fibrillar adhesin CshA has an elongated polymeric architecture.The Journal of biological chemistry · 2020Article
- Dissecting the Functional Contributions of the Intrinsically Disordered C-terminal Tail of Bacillus subtilis FtsZ.Journal of molecular biology · 2020Article
- Multidomain protein structure prediction using information about residues interacting on multimeric protein interfaces.Biophysics and physicobiology · 2020Article
- Genus trace reveals the topological complexity and domain structure of biomolecules.Scientific reports · 2018Article
- Staphylococcal Biofilms.Microbiology spectrum · 2018Review
- Self-Referential Encoding on Modules of Anticodon Pairs-Roots of the Biological Flow System.Life (Basel, Switzerland) · 2017Review
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7 authors.
Funding
Abstract
Many human proteins contain intrinsically disordered regions, and disorder in these proteins can be fundamental to their function-for example, facilitating transient but specific binding, promoting allostery, or allowing efficient posttranslational modification. SasG, a multidomain protein implicated in host colonization and biofilm formation in Staphylococcus aureus, provides another example of how disorder can play an important role. Approximately one-half of the domains in the extracellular repetitive region of SasG are intrinsically unfolded in isolation, but these E domains fold in the context of their neighboring folded G5 domains. We have previously shown that the intrinsic disorder of the E domains mediates long-range cooperativity between nonneighboring G5 domains, allowing SasG to form a long, rod-like, mechanically strong structure. Here, we show that the disorder of the E domains coupled with the remarkable stability of the interdomain interface result in cooperative folding kinetics across long distances. Formation of a small structural nucleus at one end of the molecule results in rapid structure formation over a distance of 10 nm, which is likely to be important for the maintenance of the structural integrity of SasG. Moreover, if this normal folding nucleus is disrupted by mutation, the interdomain interface is sufficiently stable to drive the folding of adjacent E and G5 domains along a parallel folding pathway, thus maintaining cooperative folding.
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