3D Structure of Phenylalanine Hydroxylase

Take a tour of Phenylalanine Hydroxylase!

Begin with a default view of the PheOH monomer. Click here.

Next lets take a look at the regions of the protein. Click here. The GREEN domain is the N terminus (aa19-117). The CYAN domain is the proposed hinge joint (111-117), and the RED domain is the C domain (118-427). The PURPLE domain is the C terminus and facilitates the binding of another PheOH monomer to make a dimer (403-427).

Let's take a look just at the C domain. Click here to see a closer view of the active site. There are 9 (8 shown) beta sheets and 13 helices in the C-terminal catalytic domain (Kobe et al. 1999).

We can get a better look at the helices and beta sheets. Click here to see the beta sheets. The YELLOW sheets are anti-parallel while the MAGENTA sheets are parallel. To see the helices, shown in VIOLET, click here. Within the C domain is a double beta-alpha-beta motif. This is a motif shared with TyrOH, TrpOH, and phosphoglycerate dehydrogenase, involved in serine biosynthesis (see previous assignments for more about similar proteins) (Kobe et al. 1999).

Now lets look just at the N regulatory terminus by clicking here. The BLUE N terminus (19-33) region is regulatory region for the C domain active sites. To see the regulatory sequence interact with the C domain active site, click here (Kobe et al. 1999).



Kobe B, et al. 1999 May. Structural basis of autoregulation of phenylalanine hydroxylase. Nature Structural Biology 6; 5: 442-8. Abstract available at <http://www.nature.com/cgi-taf/DynaPage.taf?file=/nsmb/journal/v6/n5/abs/nsb0599_442.html&dynoptions=doi1108519696>. Accessed 2005 Feb 9.

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