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  Structure of full-length transcription regulator CcpA in the apo form

Loll, B., Saenger, W., & Biesiadka, J. (2007). Structure of full-length transcription regulator CcpA in the apo form. Biochimica et Biophysica Acta-Proteins and Proteomics, 1774(6), 732-736. doi:10.1016/j.bbapap.2007.03.020.

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Genre: Journal Article
Alternative Title : Structure of full-length transcription regulator CcpA in the apo form

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BBA_1774_2007_732.pdf (Any fulltext), 520KB
 
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 Creators:
Loll, Bernhard1, Author           
Saenger, Wolfram, Author
Biesiadka, Jacek, Author
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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Free keywords: Bacillus megaterium; Carbon catabolite repression; Catabolite control protein A; DNA-binding protein; Crystal structure; Domain movement
 Abstract: 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 Å 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.

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Language(s): eng - English
 Dates: 2007-03-122007-01-132007-03-152007-04-182007-06-01
 Publication Status: Issued
 Pages: 5
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

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Title: Biochimica et Biophysica Acta-Proteins and Proteomics
  Other : BBA-Proteins Proteomics
Source Genre: Journal
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Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 1774 (6) Sequence Number: - Start / End Page: 732 - 736 Identifier: ISSN: 1570-9639
CoNE: https://pure.mpg.de/cone/journals/resource/954926938702_5