2h6c: Difference between revisions
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= cprK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=36854 Desulfitobacterium dehalogenans]) | |GENE= cprK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=36854 Desulfitobacterium dehalogenans]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[2h6b|2H6B]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2h6c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h6c OCA], [http://www.ebi.ac.uk/pdbsum/2h6c PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2h6c RCSB]</span> | |||
}} | }} | ||
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[[Category: helix-turn-helix]] | [[Category: helix-turn-helix]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:26:03 2008'' | ||
Revision as of 03:26, 31 March 2008
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| , resolution 2.90Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | cprK (Desulfitobacterium dehalogenans) | ||||||
| Related: | 2H6B
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of reduced CprK in absence of any ligand
OverviewOverview
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.
About this StructureAbout this Structure
2H6C is a Protein complex structure of sequences from Desulfitobacterium dehalogenans. 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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