Difference between revisions of "Part:BBa K352009"

Latest revision as of 15:41, 27 October 2010

P2H mutated CooA from Rhodospirillum rubrum

This part is the mutated version of CooA protein coding sequence. The mutation involves conversion proline to histidine at second amino acid. The binding strength of pCooF to CooA is expected to diminish. CooA transcriptional activator makes possible to sense CO and use CO as single energy source for Rhodospirillum rubrum and also it has heme groups.

CooA founds under a transcriptional regulators family which resembles the cAMP receptor protein and fumavate nitrate reduction from Escherichia coli. The protein functions upon in sequence-specific DNA binding when CO exists at the environment. CO dependent CooA is at the dimer structure when CO does not exist. CooA, is 28% identical (51% similar) to CRP(cAMP receptor protein) and 18% identical (45% similar) to FNR(fumavate nitrate reduction) of the Escherichia coli.

The strain has 1FT9 ID number from PDB was used for adaptation of the inactive Fe(II) CooA structure. Two monomers of the protein darkened distinctively. These monomers dimerize along the middle C-helices of adjacent effector-binding domains. Identified structure of the protein is not symmetric and one monomer has fused C- and D-helices. However, two F-helices are away from the surface structure and they act on DNA in a sequence-specific manner. The 4/5 loop, the Pro2 and His77 heme Fe(II) ligands are noted.

Terminator site was added to downstream region the gene.

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
INCOMPATIBLE WITH RFC[25]
Illegal AgeI site found at 124
1000
INCOMPATIBLE WITH RFC[1000]
Illegal SapI.rc site found at 193

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 __NOTOC__
 <partinfo>BBa_K352009 short</partinfo>
 This part is the mutated version of CooA protein coding sequence. The mutation involves conversion proline to histidine at second amino acid. The binding strength of pCooF to CooA is expected to diminish.
-CooA is a heme-containing transcriptional activator that enables Rhodospirillum rubrum to sense and grow on CO as a sole energy source.
+CooA transcriptional activator makes possible to sense CO and use CO as single energy source for Rhodospirillum rubrum and also it has heme groups.
-CooA is a member of a family of transcriptional regulators similar to the cAMP receptor protein and fumavate nitrate reduction from Escherichia coli. The protein is active in sequence-specific DNA binding in the presence of CO, but not in the absence of CO. The protein to be a dimer in the absence of CO. The product, CooA, is 28% identical (51% similar) to CRP(cAMP receptor protein) and 18% identical (45% similar) to FNR(fumavate nitrate reduction) from Escherichia coli. Inactive Fe(II) CooA structure adapted from that of the strain with PDB identification no. 1FT9. The protein consists of two monomers, shaded differently, which dimerize along the central C-helices of adjacent effector-binding domains. The solved structure is asymmetric, in which one monomer contains fused C- and D-helices. Nonetheless, both F-helices that interact with DNA in a sequence-specific manner are buried from the surface in the structure. The 4/5 loop is noted and so are the Pro2 and His77 heme Fe(II) ligands.
+CooA founds under a transcriptional regulators family which resembles the cAMP receptor protein and fumavate nitrate reduction from Escherichia coli. The protein functions upon in sequence-specific DNA binding when CO exists at the environment. CO dependent CooA is at the dimer structure when CO does not exist. CooA, is 28% identical (51% similar) to CRP(cAMP receptor protein) and 18% identical (45% similar) to FNR(fumavate nitrate reduction) of the Escherichia coli.
+The strain has 1FT9 ID number from PDB was used for adaptation of the inactive Fe(II) CooA structure. Two monomers of the protein darkened distinctively. These monomers dimerize along the middle C-helices of adjacent effector-binding domains. Identified structure of the protein is not symmetric and one monomer has fused C- and D-helices. However, two F-helices are away from the surface structure and they act on DNA in a sequence-specific manner. The 4/5 loop, the Pro2 and His77 heme Fe(II) ligands are noted.
 Terminator site was added to downstream region the gene.