Difference between revisions of "Part:BBa K1371020"

Latest revision as of 02:36, 25 October 2014

Docking domain 3 pre

The fidelity and efficiency of acyl transfer on the interfaces of the individual PKS proteins is thought to be governed by helical regions, termed Docking Domains (DD), which are located at the C-terminus of the upstream and N-terminus of downstream polypeptide chains.

This part is KS-side docking domain (KS DD) at the N-terminus of the DD3. Each DD has formed specificity of the binding because it has specific connection site. Namely each docking domain is unique in the whole polyketone synthesis pathway. With this important feature, we can ensure the connection between adjacent modules does not have randomness, which makes the product unique.

Sequence and Features

Assembly Compatibility:

10
COMPATIBLE WITH RFC[10]
12
COMPATIBLE WITH RFC[12]
21
COMPATIBLE WITH RFC[21]
23
COMPATIBLE WITH RFC[23]
25
COMPATIBLE WITH RFC[25]
1000
COMPATIBLE WITH RFC[1000]

@@ Line 1: / Line 1: @@
 __NOTOC__
 <partinfo>BBa_K1371020 short</partinfo>
-aa
+The fidelity and efficiency of acyl transfer on the interfaces of the individual PKS proteins is thought to be governed by helical regions, termed Docking Domains (DD), which are located at the C-terminus of the upstream and N-terminus of downstream polypeptide chains.
+<div class="center">
+[[File:DD-fig1 .jpg]]
+</div>
+'''This part is KS-side docking domain (KS DD) at the N-terminus of the DD3.''' Each DD has formed specificity of the binding because it has specific connection site. Namely each docking domain is unique in the whole polyketone synthesis pathway. With this important feature, we can ensure the connection between adjacent modules does not have randomness, which makes the product unique.
 <!-- Add more about the biology of this part here