2h6c: Difference between revisions

Revision as of 06:30, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2h6c.png

Template:STRUCTURE 2h6c

Crystal structure of reduced CprK in absence of any ligandCrystal structure of reduced CprK in absence of any ligand

Template:ABSTRACT PUBMED 16803881

About this StructureAbout this Structure

Full crystallographic information is available from OCA.

ReferenceReference

CprK crystal structures reveal mechanism for transcriptional control of halorespiration., Joyce MG, Levy C, Gabor K, Pop SM, Biehl BD, Doukov TI, Ryter JM, Mazon H, Smidt H, van den Heuvel RH, Ragsdale SW, van der Oost J, Leys D, J Biol Chem. 2006 Sep 22;281(38):28318-25. Epub 2006 Jun 27. PMID:16803881

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OCA

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-'''Crystal structure of reduced CprK in absence of any ligand'''
+===Crystal structure of reduced CprK in absence of any ligand===
-==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.
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 [[Category: Halorespiration]]
 [[Category: Helix-turn-helix]]
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