Functional Roles of the Charged Residues of the C- and M-Gates in the Yeast Mitochondrial NAD⁺ Transporter Ndt1p.

ABSTRACT: Mitochondrial carriers transport organic acids, amino acids, nucleotides and cofactors across the mitochondrial inner membrane. These transporters consist of a three-fold symmetric bundle of six transmembrane α-helices that encircle a pore with a central substrate binding site, whose alternating access is controlled by a cytoplasmic and a matrix gate (C- and M-gates). The C- and M-gates close by forming two different salt-bridge networks involving the conserved motifs [YF][DE]XX[KR] on the even-numbered and PX[DE]XX[KR] on the odd-numbered transmembrane α-helices, respectively. We have investigated the effects on transport of mutating the C-gate charged residues of the yeast NAD⁺ transporter Ndt1p and performed molecular docking with NAD⁺ and other substrates into str

SUBMITTER: Miniero DV 

PROVIDER: S-EPMC11677788 | biostudies-literature | 2024 Dec

REPOSITORIES: biostudies-literature