Sandbox Reserved 307: Difference between revisions
No edit summary |
No edit summary |
||
| Line 16: | Line 16: | ||
The P<sub>21</sub> structure forms a final complex consisting of six EF-Tu proteins, GDP, tetracycline, Mg<sup>2+</sup>, and 244 water molecules<ref name="gp"/>. The final complex of the P<sub>43212</sub> crystal is composed of one protein copy, GDP, tetracycline, Mg<sup>2+</sup>, SO<sub>2</sub>, glyoxylic acid, 3 Na<sup>+</sup> and 160 H2O molecules <ref name="gp"/>. In either case, the binding site for tetracycline is located in domain one, allowing it to interact with the major functional groups. Residues Tet O11 and Tet O12 of tetracycline co-ordinate Mg<sup>2+</sup><ref name="gp"/>. There is also an interaction with the phosphate of the GDP and the residues Thr25 and Asp80 <ref name="gp"/>. When bound, tetracycline replaces two well ordered water molecules from the EF-Tu structure. | The P<sub>21</sub> structure forms a final complex consisting of six EF-Tu proteins, GDP, tetracycline, Mg<sup>2+</sup>, and 244 water molecules<ref name="gp"/>. The final complex of the P<sub>43212</sub> crystal is composed of one protein copy, GDP, tetracycline, Mg<sup>2+</sup>, SO<sub>2</sub>, glyoxylic acid, 3 Na<sup>+</sup> and 160 H2O molecules <ref name="gp"/>. In either case, the binding site for tetracycline is located in domain one, allowing it to interact with the major functional groups. Residues Tet O11 and Tet O12 of tetracycline co-ordinate Mg<sup>2+</sup><ref name="gp"/>. There is also an interaction with the phosphate of the GDP and the residues Thr25 and Asp80 <ref name="gp"/>. When bound, tetracycline replaces two well ordered water molecules from the EF-Tu structure. | ||
There are three domains making up the EF-Tu molecule. <scene name='Sandbox_Reserved_307/Domain_one/1'>Domain 1</scene> <ref name="gp"/>, visualized in green, is the guanine-nucleotide domain made from residues 8-40 and 59-204. | There are three domains making up the EF-Tu molecule. <scene name='Sandbox_Reserved_307/Domain_one/1'>Domain 1</scene> <ref name="gp"/>, visualized in green, is the guanine-nucleotide domain made from residues 8-40 and 59-204. <scene name='Sandbox_Reserved_307/Domain_2/1'>Domain 2</scene>, purple, is composed on residues 205-298 and <scene name='Sandbox_Reserved_307/Domain_3/1'>Domain 3</scene> <ref name="gp"/>, yellow, of residues 299-393. The fragments 8-44 and 59-393 are associated through non-covalent interactions and retain their native conformation, with the exception of residues 40-44 and 260-263 <ref name="gp"/>. | ||
{{STRUCTURE_2hdn | PDB=2hdn | SCENE= }} | {{STRUCTURE_2hdn | PDB=2hdn | SCENE= }} | ||