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Related Concept Videos

Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

2.6K
Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
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Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

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Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
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Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

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Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
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Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

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Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to  N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
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Conserved Binding Sites01:49

Conserved Binding Sites

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Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
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Cytoskeletal Linker Proteins - Plakins01:09

Cytoskeletal Linker Proteins - Plakins

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Plakins are large proteins with binding domains for microtubules, microfilaments, intermediate filaments, and membrane-associated protein complexes at cell junctions. Plakin functions are evolutionarily conserved and are primarily involved in organizing the different components of the cytoskeleton by crosslinking them to each other and connecting them to the cell-matrix and cell adhesion complexes. They are also known to interact with signal transducers, serve as scaffolds for signaling...
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Related Experiment Video

Updated: Jul 16, 2025

Crystal Structure of the N-terminal Domain of Ryanodine Receptor from Plutella xylostella
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Crystal Structure of the N-terminal Domain of Ryanodine Receptor from Plutella xylostella

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Structures of the Insecticidal Toxin Complex Subunit XptA2 Highlight Roles for Flexible Domains.

Cole L Martin1, David W Chester1, Christopher D Radka1,2

  • 1Department of Pharmacology & Toxicology, University of Alabama at Birmingham, Birmingham, AL 35205, USA.

International Journal of Molecular Sciences
|September 9, 2023
PubMed
Summary
This summary is machine-generated.

The Toxin Complex (Tc) superfamily

Keywords:
Cryo-EMTcAX-ray crystallographytoxin translocase

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X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
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Proteomics to Identify Proteins Interacting with P2X2 Ligand-Gated Cation Channels
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Proteomics to Identify Proteins Interacting with P2X2 Ligand-Gated Cation Channels

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Related Experiment Videos

Last Updated: Jul 16, 2025

Crystal Structure of the N-terminal Domain of Ryanodine Receptor from Plutella xylostella
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Crystal Structure of the N-terminal Domain of Ryanodine Receptor from Plutella xylostella

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X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
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Proteomics to Identify Proteins Interacting with P2X2 Ligand-Gated Cation Channels
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Proteomics to Identify Proteins Interacting with P2X2 Ligand-Gated Cation Channels

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Area of Science:

  • Microbiology
  • Structural Biology
  • Biochemistry

Background:

  • The Toxin Complex (Tc) superfamily comprises toxin translocases essential for pathogenic Gram-negative bacteria.
  • The A-subunit (TcA) mediates membrane receptor targeting via its surface-exposed IgG-like receptor binding domains (RBDs).

Purpose of the Study:

  • To elucidate the structure and function of XptA2, an insect-specific TcA secreted by the nematode symbiont *X. nematophilus*.
  • To investigate the role of the linker region in XptA2 folding and conformational dynamics.

Main Methods:

  • X-ray crystallography
  • Cryo-electron microscopy (cryo-EM)
  • Biochemical analysis of protein fragments

Main Results:

  • XptA2 was determined to be pentameric, contrary to previous reports.
  • The RBD-B domain shows an indentation suggesting a potential receptor binding site or conformational trigger.
  • A two-fragment XptA2 lacking an intact linker achieved a folded pre-pore state, indicating the linker is not required for initial folding.

Conclusions:

  • The linker region in XptA2 is disordered and likely involved in dynamics after the pre-pore state.
  • Structural insights into XptA2 provide a foundation for understanding Toxin Complex function in bacterial pathogenesis.