Calcium-Induced Folding of a Beta Roll Motif Requires C-Terminal Entropic Stabilization

Blenner, Mark; Shur, Oren; Szilvay, Géza R.; Cropek, Donald M.; Banta, Scott

doi:10.1016/j.jmb.2010.04.056

Cited by 49 publications

(85 citation statements)

References 51 publications

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“…Caps may shield the hydrophobic core of the beta roll from solution, and it has been hypothesized that the C-terminal cap also acts as a nucleator of a polarized folding process which proceeds from C-terminus to N-terminus in the presence of calcium. 15 This is similar to what has been observed in other repeat proteins, such as the leucine rich repeats of internalin B, which fold in an N-terminally polarized fashion. 19 As multiple, unrelated proteins enable folding of the beta roll, we previously proposed that folding is enabled via entropic stabilization of the C-terminus.…”

Section: Introductionsupporting

confidence: 83%

“…1(a)] behaved, in solution, the same as previously characterized noncysteinemodified constructs. 15 We wanted to be sure that the presence of salt did not alter the behavior of the peptides, because a higher salt environment was required for QCM experiments, and that the addition of the cysteine amino acids could lead to dimerization which could alter the beta roll behavior. The uncapped cys-RTX and RTX-cys constructs showed no change in secondary structure by circular dichroism (CD) in up to 100 mM CaCl 2 , while the C-terminally capped cys-RTX-C construct exhibited an increase in secondary structure between 0 and 10 mM CaCl 2 , similar to what has previously been observed.…”

Section: Discussionmentioning

confidence: 99%

“…15,16 In the presence of calcium, aspartate residues in each repeat bind calcium and a beta roll structure is formed. 17,18 Folding appears to occur with the highest affinity and cooperativity when the native C-terminal sequence is present, but has also been shown to occur when other well-folded domains are fused to the C-terminus.…”

Section: Introductionmentioning

confidence: 99%

“…19 As multiple, unrelated proteins enable folding of the beta roll, we previously proposed that folding is enabled via entropic stabilization of the C-terminus. 15 Further, we reasoned that alternative nonprotein caps, including a solid surface, may be capable of enabling calcium-responsive structure formation. IDPs are a promising scaffold for engineering biomolecular recognition and will likely find utility in a variety of applications.…”

Section: Introductionmentioning

confidence: 99%

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Monitoring the conformational changes of an intrinsically disordered peptide using a quartz crystal microbalance

Shur

Banta

2011

Protein Science

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Intrinsically disordered peptides (IDPs) have recently garnered much interest because of their role in biological processes such as molecular recognition and their ability to undergo stimulus-responsive conformational changes. The block V repeat-in-toxin motif of the Bordetella pertussis adenylate cyclase is an example of an IDP that undergoes a transition from a disordered state to an ordered beta roll conformation in the presence of calcium ions. In solution, a C-terminal capping domain is necessary for this transition to occur. To further explore the conformational behavior and folding requirements of this IDP, we have cysteine modified three previously characterized constructs, allowing for attachment to the gold surface of a quartz crystal microbalance (QCM). We demonstrate that, while immobilized, the C-terminally capped peptide exhibits similar calcium-binding properties to what have been observed in solution. In addition, immobilization on the solid surface appears to enable calcium-responsiveness in the uncapped peptides, in contrast to the behavior observed in solution. This work demonstrates the power of QCM as a tool to study the conformational changes of IDPs immobilized on surfaces and has implications for a range of potential applications where IDPs may be engineered and used including protein purification, biosensors, and other bionanotechnology applications.

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Section: Introductionsupporting

confidence: 83%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Monitoring the conformational changes of an intrinsically disordered peptide using a quartz crystal microbalance

Shur

Banta

2011

Protein Science

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“…[86,92,93] The C-terminal capping structure provides the required entropic stabilization for Ca 2þ -dependent folding of the first RTX repeat segment, preventing its backwards diffusion into the cytosol. [94] The folding of the Cterminal RTX segment then triggers a translocation ratchet mechanism via segment-by-segment folding of the entire RTX domain. [5] This cooperativity results in an acceleration of the ratcheting process that allows for translocation of the Nterminal effector domain.…”

Section: Potentially Length-dependent Intramolecular Translocation Ramentioning

confidence: 99%

Bacterial Translocation Ratchets: Shared Physical Principles with Different Molecular Implementations

Hepp

Maier

2017

BioEssays

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Secretion systems enable bacteria to import and secrete large macromolecules including DNA and proteins. While most components of these systems have been identified, the molecular mechanisms of macromolecular transport remain poorly understood. Recent findings suggest that various bacterial secretion systems make use of the translocation ratchet mechanism for transporting polymers across the cell envelope. Translocation ratchets are powered by chemical potential differences generated by concentration gradients of ions or molecules that are specific to the respective secretion systems. Bacteria employ these potential differences for biasing Brownian motion of the macromolecules within the conduits of the secretion systems. Candidates for this mechanism include DNA import by the type II secretion/ type IV pilus system, DNA export by the type IV secretion system, and protein export by the type I secretion system. Here, we propose that these three secretion systems employ different molecular implementations of the translocation ratchet mechanism.

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Design of Stimuli‐Responsive Peptides and Proteins

Yang

Gerstweiler

et al. 2022

Adv Funct Materials

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Stimuli‐responsive peptides and proteins are an exciting class of smart biomaterials for various applications and have received significant attention over the past decades. A wide variety of stimuli such as temperature, pH, ions, enzymes, magnetic field, redox, etc., are explored. This article provides a review of five intensively studied types of stimuli‐responsive peptides and proteins, their design principles and applications, including temperature‐, pH‐, light‐, metal ion‐, and enzyme‐responsive with an emphasis on the key design concepts and switch function. Moreover, typical examples of their applications are discussed to provide a better understanding of the design concept and underlying methodology. This review will facilitate and inspire future innovation toward new peptide‐ and protein‐based materials and their diverse applications.

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Calcium-Induced Folding of a Beta Roll Motif Requires C-Terminal Entropic Stabilization

Cited by 49 publications

References 51 publications

Monitoring the conformational changes of an intrinsically disordered peptide using a quartz crystal microbalance

Monitoring the conformational changes of an intrinsically disordered peptide using a quartz crystal microbalance

Bacterial Translocation Ratchets: Shared Physical Principles with Different Molecular Implementations

Design of Stimuli‐Responsive Peptides and Proteins

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