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Tunnels modulate ligand flux in a heme nitric oxide/oxygen binding (h-nox) domain

Academic Article
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Overview

authors

  • Winter, M. B.
  • Herzik, M. A.
  • Kuriyan, J.
  • Marletta, Michael

publication date

  • October 2011

journal

  • Proceedings of the National Academy of Sciences of the United States of America  Journal

abstract

  • Interior topological features, such as pockets and channels, have evolved in proteins to regulate biological functions by facilitating the diffusion of biomolecules. Decades of research using the globins as model heme proteins have clearly highlighted the importance of gas pockets around the heme in controlling the capture and release of O(2). However, much less is known about how ligand migration contributes to the diverse functions of other heme protein scaffolds. Heme nitric oxide/oxygen binding (H-NOX) domains are a conserved family of gas-sensing heme proteins with a divergent fold that are critical to numerous signaling pathways. Utilizing X-ray crystallography with xenon, a tunnel network has been shown to serve as a molecular pathway for ligand diffusion. Structure-guided mutagenesis results show that the tunnels have unexpected effects on gas-sensing properties in H-NOX domains. The findings provide insights on how the flux of biomolecules through protein scaffolds modulates protein chemistry.

subject areas

  • Crystallography, X-Ray
  • Hemeproteins
  • Ligands
  • Models, Molecular
  • Mutagenesis
  • Nitric Oxide
  • Oxygen
  • Protein Conformation
  • Protein Structure, Tertiary
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Research

keywords

  • diatomic gas signaling
  • gas channels
  • hemoprotein
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Identity

PubMed Central ID

  • PMC3203760

International Standard Serial Number (ISSN)

  • 0027-8424

Digital Object Identifier (DOI)

  • 10.1073/pnas.1114038108

PubMed ID

  • 21997213
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Additional Document Info

start page

  • E881

end page

  • E889

volume

  • 108

issue

  • 43

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