Sandbox Reserved 1467

Function

Two enzymes are responsible for the oxalate that is produced in the Burkholderia species. The first enzyme, ObcA, catalyzes the formation of a tetrahedral C6-CoA adduct from the substrates acetyl-COA and oxaloacetate. The second enzyme, ObcB, produces three products from the C6-CoA adduct. These products are oxalate, acetoacetate and CoA. The oxalate produced from the Burkholderia species, is necessary for bacterial growth and maintaining environmental pH.

Disease

Species of Burkholderia can be involved in plant or human pathogenesis. Several diseases, such as B. Glumae which causes bacterial panicle blight in rice, or B. cepacia, which is an opportunistic pathogen in immunocompromised individuals, like those with cystic fibrosis or chronic granulomatous disease. It can also be involved with B. pseudomallei which can cause meliondosis, a lethal infection that leads to the formation of abscesses in internal organs.

Relevance

By studying the two mono-functional enzymes, ObcA and ObcB, there is a better understanding of the underlying molecular basis. A bifunctional enzyme, Obc 1, can be used here for oxalogenesis. Researching and finding out more about these enzymes can help advance knowledge and potentially develop ways to control diseases associated with the Burkholderia species.

Structural highlights

The of this protein is made up of mostly alpha helices, with some additional beta sheets. The of this protein has two domains, N-domain (navy) and C-Domain (gray). The two domains in this protein, Obc1, mediate oxalogenesis. The N-domain consists of an ObcB activity-exhibiting C-terminal region (Arg-529 to Gln-1106). It was found that there were no extensive interactions between the two domains, and decided to focus on the C-domain. The C-domain (Arg-530 to Gln-1106) has features common to canonical alpha/beta hydrolyses. When looking at the it is hard to distinguish between the different parts of the protein. This view can give a better insight on the size, shape, and representation of the complete molecule. The protein seems to be hydrophobic and hydrophilic. The (C3 H8 O3) is a glycerol bound structure of Obc1. Arg-935, His-1069, and Asp-997 are the residues that make up the The catalytic triad is located in the C-domain is crucial to oxalate production. A change in the catalytic triad would most likely result in loss of function of the protein. The of the C-domain in a crevice between the cap domain and the alpha/beta hydrolase fold, and the position of the catalytic Ser-935.