Search results
Results From The WOW.Com Content Network
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]
Sav1866 is a homodimer of half transporters, and each subunit contains an N-terminal TMD with six helices and a C-terminal NBD. The NBDs are similar in structure to those of other ABC transporters, in which the two ATP binding sites are formed at the dimer interface between the Walker A motif of one NBD and the LSGGQ motif of the other.
This can be done in terms of the chemical elements present, or by molecular structure e.g., water, protein, fats (or lipids), hydroxyapatite (in bones), carbohydrates (such as glycogen and glucose) and DNA. In terms of tissue type, the body may be analyzed into water, fat, connective tissue, muscle, bone, etc.
With respect to the MT-ATP6 reading frame (+3), the MT-ATP8 gene ends in the +1 reading frame with a TAG stop codon. The MT-ATP6 protein weighs 24.8 kDa and is composed of 226 amino acids . [ 8 ] [ 9 ] The protein is a subunit of the F 1 F o ATPase, also known as Complex V , which consists of 14 nuclear- and 2 mitochondrial-encoded subunits.
Domains of each subunit are also shaded differently. Two views are presented. This structure represents VCP in an ADP bound state. The N-D1 ring is larger (162 Å in diameter) than the D2 ring (113 Å) due to the laterally attached N-domains. The D1 and D2 domains are highly homologous in both sequence and structure, but they serve distinct ...
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).
The α subunit is close to the subunit b 2 and makes up the stalk that connects the transmembrane subunits to the α3β3 and δ subunits. F-ATP synthases are identical in appearance and function except for the mitochondrial F 0 F 1 -ATP synthase, which contains 7-9 additional subunits.
The yeast V-ATPase is the best characterized. There are at least thirteen subunits identified to form a functional V-ATPase complex, which consists of two domains. The subunits belong to either the V o domain (membrane associated subunits, lowercase letters on the figure) or the V 1 domain (peripherally associated subunits, uppercase letters on the figure).