3e6b

<StructureSection load='3e6b' size='340' side='right' caption='[[3e6b]], [[Resolution|resolution]] 2.01&Aring;' scene=''>

<table><tr><td colspan='2'>[[3e6b]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Deshd Deshd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E6B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3E6B FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=3C4:(3-CHLORO-4-HYDROXYPHENYL)ACETIC+ACID'>3C4</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3e5q|3e5q]], [[3e5u|3e5u]], [[3e6x|3e6x]], [[3e6c|3e6c]], [[3e6d|3e6d]]</td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Dhaf_0678 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272564 DESHD])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3e6b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e6b OCA], [http://pdbe.org/3e6b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3e6b RCSB], [http://www.ebi.ac.uk/pdbsum/3e6b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3e6b ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

Certain bacteria are able to conserve energy via the reductive dehalogenation of halo-organic compounds in a respiration-type metabolism. The transcriptional regulator CprK from Desulfitobacterium spp. induces expression of halorespiratory genes upon binding of o-chlorophenol ligands and is reversibly inactivated by oxygen through disulphide bond formation. We report crystal structures of D. hafniense CprK in the ligand-free (both oxidation states), ligand-bound (reduced) and DNA-bound states, making it the first member of the widespread CRP-FNR superfamily for which a complete structural description of both redox-dependent and allosteric molecular rearrangements is available. In conjunction with kinetic and thermodynamic ligand binding studies, we provide a model for the allosteric mechanisms underpinning transcriptional control. Amino acids that play a key role in this mechanism are not conserved in functionally distinct CRP-FNR members. This suggests that, despite significant structural homology, distinct allosteric mechanisms are used, enabling this protein family to control a very wide range of processes.

Molecular basis of halorespiration control by CprK, a CRP-FNR type transcriptional regulator.,Levy C, Pike K, Heyes DJ, Joyce MG, Gabor K, Smidt H, van der Oost J, Leys D Mol Microbiol. 2008 Oct;70(1):151-67. Epub 2008 Aug 20. PMID:18717788<ref>PMID:18717788</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 3e6b" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Deshd]]

[[Category: Levy, C]]

[[Category: Cprk]]

[[Category: Transcriptional regulator]]