SelB: Difference between revisions
No edit summary |
Eran Hodis (talk | contribs) No edit summary |
||
| Line 2: | Line 2: | ||
Elongation factor SelB uses several methods to recognize the selenocysteine insertion sequence found in messenger RNA. The insertion sequence forms a hairpin loop with an unstacked guanine base in the loop. This guanine forms | Elongation factor SelB uses several methods to recognize the selenocysteine insertion sequence found in messenger RNA. The insertion sequence forms a hairpin loop with an unstacked guanine base in the loop. This guanine forms | ||
<scene name=' | <scene name='SelB_Recognition/1wsu-recognition1/1'>specific hydrogen bonds with the protein and with two bridging water molecules (shown in cyan in the jmol).</scene> | ||
The planar base is also sandwiched between | The planar base is also sandwiched between | ||
<scene name='Sandbox_14/1wsu-recognition2/2'>three amino acids</scene> in the protein, which form a tight hydrophobic pocket. This is best seen using a | <scene name='Sandbox_14/1wsu-recognition2/2'>three amino acids</scene> in the protein, which form a tight hydrophobic pocket. This is best seen using a | ||
Revision as of 16:41, 22 July 2008
Elongation factor SelB uses several methods to recognize the selenocysteine insertion sequence found in messenger RNA. The insertion sequence forms a hairpin loop with an unstacked guanine base in the loop. This guanine forms specific hydrogen bonds with the protein and with two bridging water molecules (shown in cyan in the jmol). The planar base is also sandwiched between three amino acids in the protein, which form a tight hydrophobic pocket. This is best seen using a spacefilling diagram. The overall shape of the hairpin is recognized by contacts with several arginine and lysine amino acids. In particular, notice the intimate contact formed by both the charged nitrogen and hydrophobic carbon chain of arginine 606.
Proteopedia Page Contributors and Editors (what is this?)
David S. Goodsell, Michal Harel, Eric Martz, David Canner, Joel L. Sussman, Alexander Berchansky, Eran Hodis
