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Structural modelling of P-type ion pumps.

N M Green1, D L Stokes

  • 1National Institute for Medical Research, Mill Hill, London, U. K.

Acta Physiologica Scandinavica. Supplementum
|January 1, 1992
PubMed
Summary
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Structural analysis of P-type ion pumps reveals conserved domains and variable surface loops. Electron crystallography of the Ca++ pump provides a 3D map, supporting a conserved core model for these essential membrane proteins.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Membrane Protein Research

Background:

  • Over forty P-type ion pump sequences are known, exhibiting 20-50% sequence identity.
  • Conserved residues in P-type ion pumps are crucial for function and structure.

Purpose of the Study:

  • To analyze the conserved structural elements and functional sites of P-type ion pumps.
  • To develop a structural model for P-type ion pumps using sequence and crystallographic data.

Main Methods:

  • Sequence analysis of P-type ion pumps to identify conserved regions and domains.
  • Electron crystallography of the Ca++ pump using negative stain and amorphous ice.
  • Generation of 2D projection and 3D maps at resolutions of 6Å and 14Å, respectively.

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Main Results:

  • Identified conserved domains and variable surface loops in P-type ion pumps.
  • A structural model was assembled, correlating conserved segments with functional sites.
  • Electron crystallography provided a 14Å 3D map of the Ca++ pump, defining cytoplasmic and transmembrane domains.

Conclusions:

  • The conserved core and variable surface structure model is supported by crystallographic data.
  • The 3D map is consistent with the proposed structural model, despite limitations in functional assignment.
  • Further analysis, including tilt series, is needed for detailed 3D interpretation.