Sandbox GGC3

==Structure of Scallop Myosin 1b7t ==

<StructureSection load='1b7t' size='340' side='right' caption='Caption for this structure' scene=''>

<scene name='75/752266/Original_1b7t/1'>Original 1b7t</scene>

<scene name='75/752266/1b7t_return_scene/1'>Labeled Myosin Structure</scene>

Myosin is a type of motor protein <scene name='75/752266/1b7t_return_scene/1'>Labeled Myosin Structure</scene>, which are proteins that specialize in turning Chemical Energy to mechanical Energy. The protein is commonly found in muscle tissue and is used for motility in eukaryotes. In order for the process to work, myosin uses the subdomains in its head to locate and attach to actin filaments <scene name='75/752266/Myosin_actinattachment/1'>Overhead view of the myosin head, where the actin filament will enter.</scene> .ATP is brought into the myosin active site, where ATPase hydrolyze the ATP to ADP+Pi.The hydrolyzing leads to tighter binding of the myosin and actin filament. The ATP hydrolyze leads to a conformational change in the myosin, causing the long chain to wrap around the actin at a 45 degree angle for tighter binding<scene name='75/752266/1b7t_long_chain/2'>The long heavy chain of myosin</scene>. The release of the Pi also leads to even tighter binding. (3) The binding of myosin and actin filament forms what is known as muscle contraction or simply contractions.An additional ATP can be added to the structure to release the actin and have the cycle repeated. (1)

Common disease related to myosin is Myosin Storage Myopathy or Myopathy for short, which leads to muscle weakness.(2) The is due to mutation of the MYH7 gene that synthesizes the long heavy chain. The mutation causes clumping of the myosin protein. The clumping

stops the myosin from gathering filaments to create good contractions. The lack of this may be leading to the muscle weakness but it still unclear.

Myosin is important for eukaryotes. Without these motor proteins there would be no muscle contractions and therefore no way to mobile. Even worse, involuntary muscle such as the heart wouldn't function as well. A mutation of the protein itself as shown to lead to weakness in humans. Lack of the protein completely, would be even more detrimental.

<scene name='75/752266/Stop_scene_of_1b7t_top/1'>This scene represents zoomed in view of the labeled myosin</scene> The labels are the amino acids that make up the subunits of the myosin. Switch(Ile461-Asn470) is orange, Relay (Asn489-Asp515) is yellow, Sh1 helix(Cys693-Phe707) is cyan, Converter (707-774) is lime and the Long Heavy Chain (775-835) is black. <scene name='75/752266/1b7t_long_chain/2'>The long heavy chain of myosin</scene> <scene name='75/752266/Myosin_ball_and_stick_view/2'>This is a ball and stick model of myosin, with the head removed to identify subunits better.</scene> The colors of the label match up to the same labeling used for the ribbon model. <scene name='75/752266/Myosin_actinattachment/1'>Overhead view of the myosin head, where the actin filament will enter.</scene> (1)

(1) AnneHoudusse, Vassilios N.Kalabokis, DanielHimmel, Andrew G.Szent-Györgyi, CarolynCohen "Atomic Structure of Scallop Myosin Subfragment S1 Complexed with MgADP: A Novel Conformation of the Myosin Head":https://www.sciencedirect.com/science/article/pii/S0092867400807564 <references/>