Related Experiment Video

Updated: May 18, 2026

Crystal Structure of the N-terminal Domain of Ryanodine Receptor from Plutella xylostella
11:31

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

Published on: November 30, 2018

Crystal structure of the N-terminal domain of Nup358/RanBP2

Susanne A Kassube1, Tobias Stuwe, Daniel H Lin

  • 1Laboratory of Cell Biology, Howard Hughes Medical Institute, The Rockefeller University, 1230 York Avenue, New York, NY 10065, USA.

Journal of Molecular Biology
|September 11, 2012
PubMed

Insights

The Nup358 N-terminal domain (NTD) structure reveals an unusual conformation that binds single-stranded RNA. This finding suggests a role for the NTD in messenger ribonucleoprotein particle (mRNP) remodeling during nuclear export.

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Cell Biology

Background:

  • Messenger RNA (mRNA) export from the nucleus involves complex steps including nuclear assembly, translocation through the nuclear pore complex (NPC), and cytoplasmic remodeling.
  • Nup358/RanBP2 is a key component of the NPC's cytoplasmic filaments in higher eukaryotes, crucial for nucleocytoplasmic transport.

Purpose of the Study:

  • To determine the crystal structure of the Nup358 N-terminal domain (NTD).
  • To investigate the functional implications of the NTD structure in the context of mRNA export and mRNP remodeling.

Main Methods:

  • X-ray crystallography to determine the 0.95Å resolution structure of the Nup358 NTD.
  • Analysis of the NTD's surface electrostatic potential.
  • In vitro binding assays to assess RNA-binding capabilities.

Main Results:

  • The Nup358 NTD structure reveals an α-helical domain with three tetratricopeptide repeats (TPRs) in an extended conformation, lacking a canonical peptide-binding groove.
  • The NTD surface displays a conserved positive electrostatic potential.
  • The Nup358 NTD demonstrated the ability to bind single-stranded RNA.

Conclusions:

  • The unique structure of the Nup358 NTD suggests a non-canonical function.
  • The RNA-binding capability of the NTD points to its involvement in messenger ribonucleoprotein particle (mRNP) remodeling at the NPC's cytoplasmic face.

More Related Videos

Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae09:15

Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae

Published on: January 10, 2018

Production, Crystallization, and Structure Determination of the IKK-binding Domain of NEMO13:02

Production, Crystallization, and Structure Determination of the IKK-binding Domain of NEMO

Published on: December 28, 2019

Related Concept Videos

Directionality of Nuclear Transport01:42

Directionality of Nuclear Transport

Ras-related nuclear protein or Ran is a small G protein that cycles between its GTP and GDP bound states. Ran specific regulators, a Ran GTPase Activating Protein or RanGAP present in the cytosol and a Ran guanine nucleotide exchange factor or RanGEF present inside the nucleus regulate GTP/GDP exchange. A high concentration of GTP inside the cells, in addition to this asymmetric distribution of  Ran-specific regulators, leads to a higher RanGTP concentration inside the nucleus. This...
ATP Synthase: Structure01:18

ATP Synthase: Structure

ATP synthase or ATPase is among the most conserved proteins found in bacteria, mammals, and plants. This enzyme can catalyze a forward reaction in response to the electrochemical gradient, producing ATP from ADP and inorganic phosphate. ATP synthase can also work in a reverse direction by hydrolyzing ATP and generating an electrochemical gradient. Different forms of ATP synthases have evolved special features to meet the specific demands of the cell. Based on their specific feature, ATP...
Nuclear Export01:42

Nuclear Export

The nucleus restricts several proteins within and allows others to pass. The restricted proteins possess a nuclear retention sequence or NRS, anchoring them to the nuclear lamins and preventing their transport to the cytosol. The non-restricted proteins, after their synthesis, are transported to their site of action, such as the cytosol or other organelles, with the help of nuclear export signals or NES.
NES are of three types- the canonical 10-residue long leucine-rich signal and other...
Nucleic Acid Structure01:25

Nucleic Acid Structure

The pentose sugar in DNA is deoxyribose, while in RNA the pentose sugar is ribose. The difference between the sugars is the presence of the hydroxyl group on the ribose's second carbon and a hydrogen on the deoxyribose's second carbon. The phosphate residue attaches to the hydroxyl group of the 5′ carbon of one sugar and the hydroxyl group of the 3′ carbon of the sugar of the next nucleotide, which forms  a 5′ to 3′ phosphodiester linkage.
DNA Structure
DNA has a double-helix structure. The...
Nucleoid01:24

Nucleoid

The nucleoid represents a structurally and functionally distinct region within prokaryotic cells, where the cell's DNA and associated proteins are housed. Unlike eukaryotic cells, prokaryotes lack a membrane-bound nucleus, and the nucleoid facilitates the organization and accessibility of the genetic material within this constraint. The DNA in most bacteria and archaea exists as a single, circular, double-stranded molecule that is highly compacted through supercoiling and interactions with...
Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...