Structural clues in the sequences of the aquaporins 1 1 Edited by G. Von Heijne

Structural clues in the sequences of the aquaporins 1 1 Edited by G. Von Heijne The large number of sequences available for the aquaporin family represents a valuable source of information to incorporate into three-dimensional structure determination. Phylogenetic analysis was used to define type sequences to avoid extreme over-representation of some subfamilies, and as a measure of the quality of multiple sequence alignment. Inspection of the sequence alignment suggested eight conserved segments that define the core architecture of six transmembrane helices and two functional loops, B and E, projecting into the plane of the membrane. The sum of the core segments and the minimum lengths of the interlinking loops constitute the 208 residues necessary to satisfy the aquaporin architecture. Analysis of hydrophobic and conservation periodicity and of correlated mutations across the alignment indicated the likely assignment and orientation of the helices in the bilayer. This assignment is examined with respect to the structure of the erythrocyte aquaporin 1 determined by electron crystallography. The aquaporin 1 tetramer is described as three rings of helices, each ring with a different exposure to the lipid environment. The sequence analysis clearly suggests that two helices are exposed along their whole lengths, two helices are exposed only at their N termini, and two helices are not exposed to lipid. It is further proposed that, besides loops B and E, the highly conserved motifs on helices 1 and 4, ExxxTxxF/L, could line the water channel. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of Molecular Biology Elsevier

Structural clues in the sequences of the aquaporins 1 1 Edited by G. Von Heijne

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Publisher
Elsevier
Copyright
Copyright © 2000 Academic Press
ISSN
0022-2836
DOI
10.1006/jmbi.1999.3413
Publisher site
See Article on Publisher Site

Abstract

The large number of sequences available for the aquaporin family represents a valuable source of information to incorporate into three-dimensional structure determination. Phylogenetic analysis was used to define type sequences to avoid extreme over-representation of some subfamilies, and as a measure of the quality of multiple sequence alignment. Inspection of the sequence alignment suggested eight conserved segments that define the core architecture of six transmembrane helices and two functional loops, B and E, projecting into the plane of the membrane. The sum of the core segments and the minimum lengths of the interlinking loops constitute the 208 residues necessary to satisfy the aquaporin architecture. Analysis of hydrophobic and conservation periodicity and of correlated mutations across the alignment indicated the likely assignment and orientation of the helices in the bilayer. This assignment is examined with respect to the structure of the erythrocyte aquaporin 1 determined by electron crystallography. The aquaporin 1 tetramer is described as three rings of helices, each ring with a different exposure to the lipid environment. The sequence analysis clearly suggests that two helices are exposed along their whole lengths, two helices are exposed only at their N termini, and two helices are not exposed to lipid. It is further proposed that, besides loops B and E, the highly conserved motifs on helices 1 and 4, ExxxTxxF/L, could line the water channel.

Journal

Journal of Molecular BiologyElsevier

Published: Jan 28, 2000

References

  • The PRINTS database of protein fingerprints
    Attwood, T.K.; Avison, H.; Beck, M.E.; Bewley, M.; Bleasby, A.J.; Brewster, F.; Cooper, P.; Degtyarenko, K.; Flower, D.R.; Geddes, A.J.; Kelly, M.; Lott, S.; Measures, K.M.; Parry-Smith, D.J.; Perkins, D.N.
  • An alpha-carbon template for the transmembrane helices in the rhodopsin family of G-protein-coupled receptors
    Baldwin, J.M.; Schertler, G.F.; Unger, V.M.
  • Prediction of functional residues in water channels and related proteins
    Froger, A.; Tallur, B.; Thomas, D.; Delamarche, C.
  • Aquaporin Nt-TIPa can account for the high permeability of tobacco cell vacuolar membrane to small neutral solutes
    Gerbeau, P.; Güçlü, J.; Ripoche, P.; Maurel, C.
  • Purified lens major intrinsic protein (MIP) forms highly ordered tetragonal two-dimensional arrays by reconstitution
    Hasler, L.; Walz, T.; Tittmann, P.; Gross, H.; Kistler, J.; Engel, A.
  • Progress on the structure and function of aquaporin 1
    Heymann, J.B.; Agre, P.; Engel, A.
  • Evolution of the MIP family of integral membrane transport proteins
    Pao, G.; Wu, L.; Johnson, K.; Höfte, H.; Chrispeels, M.; Sweet, G.; Sandal, N.; Saier, M.J.
  • Structure of the water channel AqpZ from Escherichia coli revealed by electron crystallography
    Ringler, P.; Borgnia, M.J.; Stahlberg, H.; Maloney, P.C.; Agre, P.; Engel, A.
  • CLUSTAL W
    Thompson, J.D.; Higgins, D.G.; Gibson, T.J.
  • Principles of helix-helix packing in proteins
    Walther, D.; Eisenhaber, F.; Argos, P.
  • Surface topographies at subnanometer resolution reveal asymmetry and sidedness of aquaporin-1
    Walz, T.; Tittmann, P.; Fuchs, K.H.; Müller, D.J.; Smith, B.L.; Agre, P.; Gross, H.; Engel, A.

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