Sandbox Reserved 307: Difference between revisions
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The P21 structure forms a final complex consisting of six EF-Tu proteins, GDP, tetracycline, Mg2+, and 244 water molecules<ref name="gp"/>. The final complex of the P43212 crystal is composed of one protein copy, GDP, tetracycline, Mg2+, SO2, glyoxylic acid, 3 Na+ 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 Mg2+ <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 P21 structure forms a final complex consisting of six EF-Tu proteins, GDP, tetracycline, Mg2+, and 244 water molecules<ref name="gp"/>. The final complex of the P43212 crystal is composed of one protein copy, GDP, tetracycline, Mg2+, SO2, glyoxylic acid, 3 Na+ 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 Mg2+ <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. Domain 1 is the guanine-nucleotide domain made from residues 8-40 and 59-204 <scene name='Sandbox_Reserved_307/Domain_one/1'>Domain 1</scene> <ref name="gp"/>. Domain 2 is composed on residues 205-298 and | There are three domains making up the EF-Tu molecule. Domain 1 is the guanine-nucleotide domain made from residues 8-40 and 59-204 <scene name='Sandbox_Reserved_307/Domain_one/1'>Domain 1</scene> <ref name="gp"/>. Domain 2 is composed on residues 205-298 <scene name='Sandbox_Reserved_307/Domain_2/1'>Domain 2</scene> and domain 3 of residues 299-393 <scene name='Sandbox_Reserved_307/Domain_3/1'>Domain 3</scene> <ref name="gp"/>. 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"/>. | ||
In domain 1 of EF-Tu, the protein-protein interactions involved four anti-parallel β-sheet hydrogen bonds between residues 64-66’ and 66-64’ (where the primes indicate non-crystallographically related residues)<ref name="gp"/>. Hydrogen bonds are also formed between the side chain of Asn63 and Glu68 as well as the main chain residues Ile62 with His66 and Glu60 <ref name="gp"/>. | In domain 1 of EF-Tu, the protein-protein interactions involved four anti-parallel β-sheet hydrogen bonds between residues 64-66’ and 66-64’ (where the primes indicate non-crystallographically related residues)<ref name="gp"/>. Hydrogen bonds are also formed between the side chain of Asn63 and Glu68 as well as the main chain residues Ile62 with His66 and Glu60 <ref name="gp"/>. | ||