3e6d: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
m Protected "3e6d" [edit=sysop:move=sysop]
No edit summary
Line 1: Line 1:
[[Image:3e6d.png|left|200px]]
==Crystal Structure of CprK C200S==
<StructureSection load='3e6d' size='340' side='right' caption='[[3e6d]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3e6d]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Desulfitobacterium_hafniense Desulfitobacterium hafniense]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E6D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3E6D FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3e5q|3e5q]], [[3e5u|3e5u]], [[3e6x|3e6x]], [[3e6b|3e6b]], [[3e6c|3e6c]]</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=49338 Desulfitobacterium hafniense])</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=3e6d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e6d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3e6d RCSB], [http://www.ebi.ac.uk/pdbsum/3e6d PDBsum]</span></td></tr>
</table>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e6/3e6d_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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.


{{STRUCTURE_3e6d|  PDB=3e6d  |  SCENE=  }}
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>


===Crystal Structure of CprK C200S===
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
{{ABSTRACT_PUBMED_18717788}}
== References ==
 
<references/>
==About this Structure==
__TOC__
[[3e6d]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Desulfitobacterium_hafniense Desulfitobacterium hafniense]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E6D OCA].
</StructureSection>
 
==Reference==
<ref group="xtra">PMID:018717788</ref><references group="xtra"/>
[[Category: Desulfitobacterium hafniense]]
[[Category: Desulfitobacterium hafniense]]
[[Category: Levy, C.]]
[[Category: Levy, C]]
[[Category: Cprk]]
[[Category: Cprk]]
[[Category: Halorespiration]]
[[Category: Halorespiration]]
[[Category: Transcription regulation]]
[[Category: Transcription regulation]]
[[Category: Transcriptional regulator]]
[[Category: Transcriptional regulator]]

Revision as of 16:14, 19 November 2014

Crystal Structure of CprK C200SCrystal Structure of CprK C200S

Structural highlights

3e6d is a 2 chain structure with sequence from Desulfitobacterium hafniense. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:Dhaf_0678 (Desulfitobacterium hafniense)
Resources:FirstGlance, OCA, RCSB, PDBsum

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Levy C, Pike K, Heyes DJ, Joyce MG, Gabor K, Smidt H, van der Oost J, Leys D. Molecular basis of halorespiration control by CprK, a CRP-FNR type transcriptional regulator. Mol Microbiol. 2008 Oct;70(1):151-67. Epub 2008 Aug 20. PMID:18717788 doi:10.1111/j.1365-2958.2008.06399.x

3e6d, resolution 2.00Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA