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Related Concept Videos

Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Cooperative Binding of Transcription Regulators02:13

Cooperative Binding of Transcription Regulators

Transcriptional regulators bind to specific cis-regulatory sequences in the DNA to regulate gene transcription. These cis-regulatory sequences are very short, usually less than ten nucleotide pairs in length. The short length means that there is a high probability of the exact same sequence randomly occurring throughout the genome.  Since regulators can also bind to groups of similar sequences, this further increases the chances of random binding. Transcriptional regulators form dimers that...
Cooperative Binding of Transcription Regulators02:13

Cooperative Binding of Transcription Regulators

Transcriptional regulators bind to specific cis-regulatory sequences in the DNA to regulate gene transcription. These cis-regulatory sequences are very short, usually less than ten nucleotide pairs in length. The short length means that there is a high probability of the exact same sequence randomly occurring throughout the genome.  Since regulators can also bind to groups of similar sequences, this further increases the chances of random binding. Transcriptional regulators form dimers that...
The Supercomplexes in the Crista Membrane01:41

The Supercomplexes in the Crista Membrane

The mitochondrial cristae membrane is the primary site for the oxidative phosphorylation (OXPHOS) process of energy conversion mediated through respiratory complexes I to V. These complexes have been widely studied for decades, and it has been proven that they form supramolecular structures called respiratory supercomplexes (SC). These higher-order complexes may be crucial in maintaining the biochemical structure and improving the physiological activity of the individual complexes while...

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Structural basis for cooperativity of CRM1 export complex formation.

Thomas Monecke1, David Haselbach, Béla Voß

  • 1Abteilung für Molekulare Strukturbiologie, Institut für Mikrobiologie und Genetik, Göttinger Zentrum für Molekulare Biowissenschaften, Georg-August-Universität Göttingen, D-37077 Göttingen, Germany.

Proceedings of the National Academy of Sciences of the United States of America
|January 2, 2013
PubMed
Summary

Free chromosome region maintenance 1 (CRM1) exportin adopts an extended, superhelical shape, not a compact ring. This conformation change regulates cargo binding and nuclear export, revealing CRM1

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Area of Science:

  • Molecular biology
  • Cell biology
  • Structural biology

Background:

  • Nuclear transport receptors, like exportins, mediate macromolecule movement between the nucleus and cytoplasm in eukaryotes.
  • Chromosome region maintenance 1 (CRM1) is a key exportin, crucial for the nuclear export of diverse proteins and ribonucleoproteins.
  • CRM1 was previously thought to maintain a toroidal (ring-like) structure throughout the entire nuclear transport cycle.

Purpose of the Study:

  • To determine the structure of free CRM1 and understand its conformational dynamics.
  • To elucidate the mechanism by which CRM1 regulates cargo binding and nuclear export.
  • To propose a model for CRM1 export complex assembly and allosteric regulation.

Main Methods:

  • X-ray crystallography of free CRM1 from Chaetomium thermophilum.
  • Single-particle electron microscopy (EM) to analyze CRM1 conformation in solution.
  • Molecular dynamics (MD) simulations to study conformational transitions and regulatory roles.

Main Results:

  • Crystal structures revealed that unbound CRM1 adopts an extended, pitched superhelical conformation, differing significantly from its complexed state.
  • EM analysis showed free CRM1 exists in an equilibrium between extended and compact, ring-like forms.
  • MD simulations identified the C-terminal helix as crucial for regulating the conformational transition and modulating cargo-binding sites.

Conclusions:

  • CRM1 is conformationally dynamic, transitioning between extended and compact states.
  • These conformational changes are critical for regulating nuclear export signal binding and cargo association.
  • A model for CRM1 export complex assembly is proposed, highlighting long-range allosteric communication between Ran and cargo binding sites.