2hsg: Difference between revisions

Revision as of 18:45, 21 February 2008

Structure of transcription regulator CcpA in its DNA-free state

OverviewOverview

The catabolite control protein A (CcpA) from Bacillus megaterium is a member of the bacterial repressor protein family GalR-LacI. CcpA functions as master transcriptional regulator of carbon catabolite repression/regulation in firmicutes. Here we present the crystal structure of full-length apo CcpA at 2.5 A resolution from B. megaterium. The structure reveals the location of the helix-turn-helix domain as well as the hinge region, which were not visible due to their high flexibility in earlier crystallographic studies on CcpA molecules. The structure of the apo CcpA homodimer in the present form is in contrast to other reported structures for CcpA.

About this StructureAbout this Structure

2HSG is a Single protein structure of sequence from Bacillus megaterium. Full crystallographic information is available from OCA.

ReferenceReference

Structure of full-length transcription regulator CcpA in the apo form., Loll B, Saenger W, Biesiadka J, Biochim Biophys Acta. 2007 Jun;1774(6):732-6. Epub 2007 Apr 18. PMID:17500051

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 ==Overview==
-The catabolite control protein A (CcpA) from Bacillus megaterium is a, member of the bacterial repressor protein family GalR-LacI. CcpA functions, as master transcriptional regulator of carbon catabolite, repression/regulation in firmicutes. Here we present the crystal structure, of full-length apo CcpA at 2.5 A resolution from B. megaterium. The, structure reveals the location of the helix-turn-helix domain as well as, the hinge region, which were not visible due to their high flexibility in, earlier crystallographic studies on CcpA molecules. The structure of the, apo CcpA homodimer in the present form is in contrast to other reported, structures for CcpA.
+The catabolite control protein A (CcpA) from Bacillus megaterium is a member of the bacterial repressor protein family GalR-LacI. CcpA functions as master transcriptional regulator of carbon catabolite repression/regulation in firmicutes. Here we present the crystal structure of full-length apo CcpA at 2.5 A resolution from B. megaterium. The structure reveals the location of the helix-turn-helix domain as well as the hinge region, which were not visible due to their high flexibility in earlier crystallographic studies on CcpA molecules. The structure of the apo CcpA homodimer in the present form is in contrast to other reported structures for CcpA.
 ==About this Structure==
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 ==Reference==
-Structure of full-length transcription regulator CcpA in the apo form., Loll B, Saenger W, Biesiadka J, Biochim Biophys Acta. 2007 Apr 18;. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17500051 17500051]
+Structure of full-length transcription regulator CcpA in the apo form., Loll B, Saenger W, Biesiadka J, Biochim Biophys Acta. 2007 Jun;1774(6):732-6. Epub 2007 Apr 18. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17500051 17500051]
 [[Category: Bacillus megaterium]]
 [[Category: Single protein]]
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 [[Category: transcriptional regulator]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 14:52:47 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:45:14 2008''