Abstract:
:Mitochondrial porin facilitates the diffusion of small hydrophilic molecules across the mitochondrial outer membrane. Despite low sequence similarity among porins from different species, a "glycine-leucine-lysine" (GLK) motif is conserved in mitochondrial and Neisseria porins. To investigate the possible roles of these conserved residues, including their hypothesized participation in ATP binding by the protein, we replaced the lysine residue of the GLK motif of Neurospora crassa porin with glutamic acid through site-directed mutagenesis of the corresponding gene. Although the pores formed by this protein have size and gating characteristics similar to those of the wild-type protein, the channels formed by GLEporin are less anion selective than the wild-type pores. The GLEporin retains the ability to be cross linked to [alpha-(32)P]ATP, indicating that the GLK sequence is not essential for ATP binding. Furthermore, the pores formed by both GLEporin and the wild-type protein become more cation selective in the presence of ATP. Taken together, these results support structural models that place the GLK motif in a part of the ion-selective beta-barrel that is not directly involved in ATP binding.
journal_name
J Bioenerg Biomembrjournal_title
Journal of bioenergetics and biomembranesauthors
Runke G,Maier E,O'Neil JD,Benz R,Court DAdoi
10.1023/a:1005618510502keywords:
subject
Has Abstractpub_date
2000-12-01 00:00:00pages
563-70issue
6eissn
0145-479Xissn
1573-6881pii
291202journal_volume
32pub_type
杂志文章abstract::The role of nucleoside diphosphate (NDP) kinase with special reference to mammalian signal transduction systems was described. The interaction between NDP kinases and G proteins was reevaluated in view of their protein structural information and its significance was extended further on the basis of recent findings obt...
journal_title:Journal of bioenergetics and biomembranes
pub_type: 杂志文章,评审
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journal_title:Journal of bioenergetics and biomembranes
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journal_title:Journal of bioenergetics and biomembranes
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journal_title:Journal of bioenergetics and biomembranes
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journal_title:Journal of bioenergetics and biomembranes
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journal_title:Journal of bioenergetics and biomembranes
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journal_title:Journal of bioenergetics and biomembranes
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journal_title:Journal of bioenergetics and biomembranes
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journal_title:Journal of bioenergetics and biomembranes
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journal_title:Journal of bioenergetics and biomembranes
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journal_title:Journal of bioenergetics and biomembranes
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journal_title:Journal of bioenergetics and biomembranes
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