Sandbox Reserved 479: Difference between revisions
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{{STRUCTURE_2mys| PDB=2mys | SCENE= }} | {{STRUCTURE_2mys| PDB=2mys | SCENE= }} | ||
Proteolytic fragment of myosin generated by papain digestion in ''Gallus gallus'' (chicken) bound to ligands <scene name='Sandbox_Reserved_479/2_mys_magnesium_ligand/2'>magnesium</scene> and <scene name='Sandbox_Reserved_479/2_mys_sulfate_ion/1'>sulfate ion</scene> | |||
==Structure== | ==Structure== | ||
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The actin-binding, <scene name='Sandbox_Reserved_479/2mys_active_site/1'>catalytic site</scene> of myosin is known as S1 (subfragment 1). This is the amino-terminal globular head portion of the myosin molecule. The S1 head is divided into three subdomains: the NH2-terminal 25 kDa region, a central 50 kDa region, and the COOH-terminal 20 kDa region. Further analysis of the S1 active site of myosin suggests that the γ-phosphate (of ATP) binds near the apex of the 50 kDa cleft. It is believed to be a region critical to function, because of the presence of evolutionarily conserved residues along the central cleft.<ref name="Ruppel" /> The actin-binding site and nucleotide-binding site, although dominated by alpha-helices, also contains a straightened section with two cysteine residues. The can form a disulfide bond in the presence of a nucleotide that prevents ADP from leaving the active site.<ref name="CHEM43" /> | The actin-binding, <scene name='Sandbox_Reserved_479/2mys_active_site/1'>catalytic site</scene> of myosin is known as S1 (subfragment 1). This is the amino-terminal globular head portion of the myosin molecule. The S1 head is divided into three subdomains: the NH2-terminal 25 kDa region, a central 50 kDa region, and the COOH-terminal 20 kDa region. Further analysis of the S1 active site of myosin suggests that the γ-phosphate (of ATP) binds near the apex of the 50 kDa cleft. It is believed to be a region critical to function, because of the presence of evolutionarily conserved residues along the central cleft.<ref name="Ruppel" /> The actin-binding site and nucleotide-binding site, although dominated by alpha-helices, also contains a straightened section with two cysteine residues. The can form a disulfide bond in the presence of a nucleotide that prevents ADP from leaving the active site.<ref name="CHEM43" /> | ||
====X-Ray Crystallography and Diffraction==== | ====X-Ray Crystallography and Diffraction==== | ||
