Sandbox 3

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Binding sites of Torpedo acetylcholinesterase (EC 3.1.1.7) with the bisquaternary ligand decamethonium (DME). DME is oriented along the narrow gorge leading to the active site; one quaternary group is apposed to the indole of W84 and the other to that of W279, near the top of the gorge, i.e. the "peripheral" anionic site. The only major conformational change in the structure AChE is in the orientation of F330 which lies parallel to the surface of the gorge, near the cationic binding site of AChE which contains the catalytic triad S200, E327 & H440.
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[[Image:1ema.gif|thumb|left|350px|Green fluorescent protein (1ema)]]
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Green fluorescent protein ('''GFP'''), originally isolated from the jellyfish Aequorea victoria (PDB entry [[1ema]]), fluorsceses green (509nm) when exposed to blue light (395nm and 475nm). It is one of the most important proteins used in biological research because it can be used to tag otherwise invisible gene products of interest and thus observe their existence, location and movement.
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== Exploring the Structure ==
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<applet load='1ema' size='300' frame='true' align='right' caption='Insert caption here' />
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GFP is a beta barrel protein with 11 beta sheets. It is a 26.9kDa protein made up of 238 amino acids. The <scene name='Sandbox_3/1ema_chromophore/1'>chromophore</scene>, responsible for the fluorescent properties of the protein, is buried inside the beta barrel as part of the central alpha helix passing through the barrel. The chromophore forms via spontaneous cyclization and oxidation of three residues in the central alpha helix: -Thr65 (or Ser65)-Tyr66-Gly67. This cyclization and oxidation creates the chromophore's five-membered ring via a new bond between the threonine and the glycine residues.<ref>PMID:8703075</ref>
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<references/>
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Current revision

Green fluorescent protein (1ema)
Green fluorescent protein (1ema)

Green fluorescent protein (GFP), originally isolated from the jellyfish Aequorea victoria (PDB entry 1ema), fluorsceses green (509nm) when exposed to blue light (395nm and 475nm). It is one of the most important proteins used in biological research because it can be used to tag otherwise invisible gene products of interest and thus observe their existence, location and movement.

Exploring the Structure

Insert caption here

Drag the structure with the mouse to rotate

GFP is a beta barrel protein with 11 beta sheets. It is a 26.9kDa protein made up of 238 amino acids. The , responsible for the fluorescent properties of the protein, is buried inside the beta barrel as part of the central alpha helix passing through the barrel. The chromophore forms via spontaneous cyclization and oxidation of three residues in the central alpha helix: -Thr65 (or Ser65)-Tyr66-Gly67. This cyclization and oxidation creates the chromophore's five-membered ring via a new bond between the threonine and the glycine residues.[1]

  1. ↑ Ormo M, Cubitt AB, Kallio K, Gross LA, Tsien RY, Remington SJ. Crystal structure of the Aequorea victoria green fluorescent protein. Science. 1996 Sep 6;273(5280):1392-5. PMID:8703075



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