This is a default text for your page '. Click above on edit this page' to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia [1] or to the article describing Jmol [2] to the rescue.
Function
Mechanism
The structure of this protein comprises of two prominent domains. The larger one contains an N terminal distorted beta-barrel accompanied by alpha helices. The second and smaller unit is consist of a beta sheet and alpha helix complex (Viviani, 2002). The process of fluorescence is achieved through a two-step oxidation reaction involving the substrate Lucinferin accompanied with ATP, Magnesium and oxygen. The first step consist of using ATP-Mg in an Acylation reaction of the COOH group on Lucinferin producing a Luciferyl adenylate intermediate and a phosphate group. The second reaction uses oxygen to create an excited state of the molecule. The molecule then returns to its ground state emitting a photon of light (Conti et al., 1996). A single peptide has been discover that plays a vital role in the photooxidation by Luciferase. The specific amino acid is a histidine located in the region 244HHGF247 of the protein (Branchini, 1997). It has been shown to be necessary for the use of oxygen in the second part of the reaction.
Disease
Relevance
Structural highlights
This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
