Ure of -barrels is dictated by the hydrogen-bonded network, resulting inside a steady tertiary arrangement, helix-helix contacts in the membrane involve weak packing interactions. Accordingly, these two varieties of proteins are extremely differently sensitive to theDOI: ten.1021/acs.chemrev.7b00570 Chem. Rev. 2018, 118, 3559-Chemical ReviewsReviewFigure six. Amino acid sequences plus the structures with the mitochondrial ADP/ATP carrier AAC1 and uncoupling protein UCP2. (A) Aligned amino acid sequences of bovine AAC1 and mouse UCP2, shown in the ZAPPO colour scheme making use of the program Jalview.151 Identical residues are shown inside the consensus sequence and are indicated by black boxes. Also indicated will be the positions from the matrix147 and cytoplasmic152 bridge networks. Mitochondrial carriers consist of 3 homologous sequence repeats, that are aligned beneath each other. (B) Cytoplasmic and (C) lateral views of the structures of bovine AAC1 (1OKC) determined by X-ray crystallography (left)147 and mouse UCP2 (2LCK) determined by resolution NMR (right).118 The odd-numbered -helices (H1, H3, H5), matrix -helices (h12, h34, h56), and even-numbered -helices (H2, H4, H6) are shown in green, blue, and red cartoon representations, respectively. Symmetry-related glycine residues in the EG-motif are shown in black spheres, whereas the residues on the matrix salt bridge network, which are interacting in these states (cyan dashes), are shown in yellow sticks. The 3-fold pseudosymmetrical axis is shown by a triangle.membrane/detergent environment, and are discussed 1123231-07-1 Data Sheet separately in this section.four.1. -Helical Membrane Proteins4.1.1. Mitochondrial Carriers. The mitochondrial carrier family members (MCF) delivers numerous examples that reveal effects ofDPC on membrane protein structure and dynamics. Mitochondrial carriers (MCs) shuttle unique classes of substrates, like keto acids, amino acids, nucleotides, inorganic ions, and cofactors, across the inner mitochondrial membrane.132-134 The amino acid sequences of MCs comprise 3 homologousDOI: ten.1021/acs.chemrev.7b00570 Chem. Rev. 2018, 118, 3559-Chemical ReviewsReviewFigure 7. Structures of AAC (in DDM or LAPAO) and UCP2 (in DPC) have pretty various options. (A) Distribution from the axial interhelical distances of the bovine mitochondrial ADP/ATP carrier AAC147(wheat) and uncoupling protein UCP2118 (green). The dotted lines indicate the average values. (B) Cross-section via the middle from the bovine AAC1 (left) and mouse UCP2 (proper) structures. AAC1 includes a layer of about 20 to prevent the leak of protons, whereas UCP2 has a hole via the whole protein, which can be substantial sufficient for tiny molecules and protons to pass through from the intermembrane space towards the mitochondrial matrix and would short-circuit the mitochondrion. (C) Cross-sectional view of UCP2 in complicated with GDP2- in MD simulations in explicit DPC.120 The detergent is organized inside a bundle around the hydrophobic core, at the same time as in two extra micelles, assembled around the matrix and cytoplasmic sides around amphiphilic patches of amino acids. The internal cavity with the protein is completely opened on both sides in the protein and filled by a big quantity of water molecules. (D) Surface representation of UCP2 following 200 ns of MD simulation in explicit DPC, applying the NMR structure as starting conformation. For clarity, ions, water molecules, and detergents are usually not shown. The lateral openings in between helices is usually clearly noticed.repeats of ca. 100 residues.135 In light of.
