http://www.cnr.it/ontology/cnr/individuo/prodotto/ID12802
Functional and structural role of amino acid residues in the even-numbered transmembrane á-helices of the bovine mitochondrial oxoglutarate carrier. (Articolo in rivista)
- Type
- Label
- Functional and structural role of amino acid residues in the even-numbered transmembrane á-helices of the bovine mitochondrial oxoglutarate carrier. (Articolo in rivista) (literal)
- Anno
- 2006-01-01T00:00:00+01:00 (literal)
- Alternative label
A.R. Cappello, R. Curcio, D.V. Miniero, I. Stipani, A.J. Robinson, E. R. S. Kunji and F. Palmieri (2006)
Functional and structural role of amino acid residues in the even-numbered transmembrane á-helices of the bovine mitochondrial oxoglutarate carrier.
in Journal of Molecular Biology
(literal)
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- A.R. Cappello, R. Curcio, D.V. Miniero, I. Stipani, A.J. Robinson, E. R. S. Kunji and F. Palmieri (literal)
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- Rivista
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- ISI Web of Science (WOS) (literal)
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- Laboratory of Biochemistry and Molecular Biology, Department of Pharmaco-Biology, University of Bari, Via Orabona 4, 70125 Bari, Italy
University of Calabria, Via P.Bucci , 87036 Arcavacata di Rende (CS), Italy (literal)
- Titolo
- Functional and structural role of amino acid residues in the even-numbered transmembrane á-helices of the bovine mitochondrial oxoglutarate carrier. (literal)
- Abstract
- The mitochondrial oxoglutarate carrier exchanges cytosolic malate for 2-
oxoglutarate from the mitochondrial matrix. Orthologs of the carrier have
a high degree of amino acid sequence conservation, meaning that it is
impossible to identify residues important for function on the basis of this
criterion alone. Therefore, each amino acid residue in the transmembrane
á-helices H2 and H6 was replaced by a cysteine in a functional
mitochondrial oxoglutarate carrier that was otherwise devoid of cysteine
residues. The effects of the cysteine replacement and subsequent
modification by sulfhydryl reagents on the initial uptake rate of 2-
oxoglutarate were determined. The results were evaluated using a
structural model of the oxoglutarate carrier. Residues involved in interhelical
and lipid bilayer interactions tolerate cysteine replacements or their
modifications with little effect on transport activity. In contrast, the
majority of cysteine substitutions in the aqueous cavity had a severe effect
on transport activity. Residues important for function of the carrier cluster
in three regions of the transporter. The first consists of residues in the
[YWLF]- [KR]-G-X-X-P sequence motif, which is highly conserved in all
members of the mitochondrial carrier family. The residues may fulfill a
structural role as a helix breaker or a dynamic role as a hinge region for
conformational changes during translocation. The second cluster of
important residues can be found at the carboxy-terminal end of the
even-numbered transmembrane á-helices at the cytoplasmic side of the
carrier. Residues in H6 at the interface with H1 are the most sensitive to
mutation and modification, and may be essential for folding of the carrier
during biogenesis. The third cluster is at the midpoint of the membrane
and consists of residues that are proposed to be involved in substrate
binding. (literal)
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