Difference between revisions of "Part:BBa K1615111"

Revision as of 23:28, 21 September 2015

CBDcipA with N and C-terminal linker in RFC25

Cellulose binding domains (CBDs) mediate the binding of enzymes to cellulose¹. CBDs are divided into over a dozen families based on their sequence homology ². Family III of CBDs is divided into a, b and c with CBDCipA belonging to family III a; the clostridial scaffoldin CBDs³. CBDCipA was identified in Clostridium thermocellum and is capable of binding to crystalline cellulose in a reversible manner⁴. CBDCipA includes endogenous linker sequences at both the N and C-terminals which help to prevent the CBD from interfering with the folding of any other protein it may be fused to.

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]

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 __NOTOC__
 <partinfo>BBa_K1615111 short</partinfo>
-CBDcipA with endogenous N and C terminal linkers from Clostridium thermocellum. This part is an improved version of BBa_K1321014, eliminating the illegal EcoRI site. This part is now BioBrick compatible using RFC25.
+Cellulose binding domains (CBDs) mediate the binding of enzymes to cellulose<sup>1</sup>. CBDs are divided into over a dozen families based on their sequence homology <sup>2</sup>. Family III of CBDs is divided into a, b and c with CBDCipA belonging to family III a; the clostridial scaffoldin CBDs<sup>3</sup>. CBDCipA was identified in <i>Clostridium thermocellum</i> and is capable of binding to crystalline cellulose in a reversible manner<sup>4</sup>. CBDCipA includes endogenous linker sequences at both the N and C-terminals which help to prevent the CBD from interfering with the folding of any other protein it may be fused to.
 <!-- Add more about the biology of this part here