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| {{STRUCTURE_2h6c| PDB=2h6c | SCENE= }} | | {{STRUCTURE_2h6c| PDB=2h6c | SCENE= }} |
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| '''Crystal structure of reduced CprK in absence of any ligand'''
| | ===Crystal structure of reduced CprK in absence of any ligand=== |
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| ==Overview==
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| Halorespiration is a bacterial respiratory process in which haloorganic compounds act as terminal electron acceptors. This process is controlled at transcriptional level by CprK, a member of the ubiquitous CRP-FNR family. Here we present the crystal structures of oxidized CprK in presence of the ligand ortho-chlorophenolacetic acid and of reduced CprK in absence of this ligand. These structures reveal that highly specific binding of chlorinated, rather than the corresponding non-chlorinated, phenolic compounds in the NH(2)-terminal beta-barrels causes reorientation of these domains with respect to the central alpha-helix at the dimer interface. Unexpectedly, the COOH-terminal DNA-binding domains dimerize in the non-DNA binding state. We postulate the ligand-induced conformational change allows formation of interdomain contacts that disrupt the DNA domain dimer interface and leads to repositioning of the helix-turn-helix motifs. These structures provide a structural framework for further studies on transcriptional control by CRP-FNR homologs in general and of halorespiration regulation by CprK in particular.
| | The line below this paragraph, {{ABSTRACT_PUBMED_16803881}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 16803881 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_16803881}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Halorespiration]] | | [[Category: Halorespiration]] |
| [[Category: Helix-turn-helix]] | | [[Category: Helix-turn-helix]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:55:04 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 06:30:18 2008'' |