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Updated: Dec 20, 2025

Spatio-Temporal Manipulation of Small GTPase Activity at Subcellular Level and on Timescale of Seconds in Living Cells
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Published on: March 9, 2012

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Conformational Dynamics from Ambiguous Zinc Coordination in the RanBP2-Type Zinc Finger of RBM5

Komal Soni1, Santiago Martínez-Lumbreras1, Michael Sattler1

  • 1Institute of Structural Biology, Helmholtz Zentrum München, Ingolstädter Landstrasse 1, 85764 Neuherberg, Germany; Center for Integrated Protein Science Munich at Bavarian NMR Center and Biomolecular NMR, Department Chemie, Technical University of Munich, Lichtenbergstrasse 4, 85748 Garching, Germany.

Journal of Molecular Biology
|May 26, 2020
PubMed

Insights

The RBM5 protein

Area of Science:

  • Molecular biology
  • Biochemistry
  • Structural biology

Background:

  • RBM5 protein is a biomarker for metastasis.
  • RBM5 influences alternative splicing of apoptotic genes like Fas and Caspase-2.
  • The RBM5 RanBP2-type zinc finger (Zf1) binds single-stranded RNA.

Purpose of the Study:

  • Investigate the structure and dynamics of the human RBM5 Zf1 domain.
  • Understand the role of a non-canonical cysteine in Zf1 stability and function.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy.
  • Metal-exchange kinetics studies.
  • Protein mutation analysis.

Main Results:

  • The non-canonical cysteine in RBM5 Zf1 kinetically destabilizes the protein.
  • Mutating this cysteine enhances high-affinity zinc coordination.
  • Structural instability may facilitate functional adaptation.

Conclusions:

  • The RBM5 Zf1 domain's structure is influenced by a non-canonical cysteine.
  • Altering zinc coordination through mutation impacts protein stability.
  • Evolutionary selection of destabilizing mutations can lead to functional protein adaptation.
Keywords:
NMRRBM5RanBP2 Zinc fingermetal-exchange kinetics

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