期刊
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
卷 367, 期 1, 页码 60-66出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2007.12.079
关键词
Nodulin 26; aquaporin; three-dimensional model; legume plants; nitrogen-fixation symbiosis
The three-dimensional models built for the Nod26-like aquaporins all exhibit the typical alpha-helical fold of other aquaporins containing the two ar/R and NPA constriction filters along the central water channel. Besides these structural homologies, they readily differ with respect to the amino acid residues forming the ar/R selective filter. According to these discrepancies in both the hydrophilicity and pore size of the ar/R filter, Nod26-like aquaporins can be distributed in three subgroups corresponding to NIP-1, NIP-II and a third subgroup of Nod26-like aquaporins exhibiting a highly hydrophilic and widely open filter. However, all Nod26-like aquaporins display a bipartite distribution of electrostatic charges along the water channel with an electropositive extracellular vestibular portion followed by an electronegative cytosolic vestibular portion. The specific transport of water, non-ionic solutes (glycerol, urea, ammoniac), ions (NH4+) and gas (NH3) across the Nod26-like obviously depends on the electrostatic and conformational properties of their central water channel. (C) 2007 Elsevier Inc. All rights reserved.
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