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MT-ATP8 (or ATP8) is a mitochondrial gene with the full name 'mitochondrially encoded ATP synthase membrane subunit 8' that encodes a subunit of mitochondrial ATP synthase, ATP synthase F o subunit 8 (or subunit A6L). This subunit belongs to the F o complex of the large, transmembrane F-type ATP synthase. [5]
The structure of the intact ATP synthase is currently known at low-resolution from electron cryo-microscopy (cryo-EM) studies of the complex. The cryo-EM model of ATP synthase suggests that the peripheral stalk is a flexible structure that wraps around the complex as it joins F 1 to F O.
Prenylation (also known as isoprenylation or lipidation) is the addition of hydrophobic molecules to a protein or a biomolecule. It is usually assumed that prenyl groups (3-methylbut-2-en-1-yl) facilitate attachment to cell membranes , similar to lipid anchors like the GPI anchor , though direct evidence of this has not been observed.
Also, the structure of the T domains determines the specificity of each ABC protein. In the inward facing conformation, the binding site on the A domain is open directly to the surrounding aqueous solutions. This allows hydrophilic molecules to enter the binding site directly from the inner leaflet of the phospholipid bilayer. In addition, a ...
The human MT-ATP6 gene, located in mitochondrial DNA, is 681 base pairs in length. [7] An unusual feature of MT-ATP6 is the 46-nucleotide gene overlap of its first codons with the end of the MT-ATP8 gene. With respect to the MT-ATP6 reading frame (+3), the MT-ATP8 gene ends in the +1 reading frame with a TAG stop codon.
Structure of a flippase, showing the two major subunits of the enzyme. Flippases are transmembrane lipid transporter proteins located in the cell membrane.They are responsible for aiding the movement of phospholipid molecules between the two layers, or leaflets, that compose the membrane (transverse diffusion, also known as a "flip-flop" transition).
Within chromosomes, DNA is held in complexes with structural proteins. These proteins organize the DNA into a compact structure called chromatin. In eukaryotes, this structure involves DNA binding to a complex of small basic proteins called histones. In prokaryotes, multiple types of proteins are involved.
DNA gyrase, or simply gyrase, is an enzyme within the class of topoisomerase and is a subclass of Type II topoisomerases [1] that reduces topological strain in an ATP dependent manner while double-stranded DNA is being unwound by elongating RNA-polymerase [2] or by helicase in front of the progressing replication fork.