2fbk
From Proteopedia
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| - | [[Image:2fbk.gif|left|200px]] | + | [[Image:2fbk.gif|left|200px]] |
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| - | '''The Crystal Structure of HucR from Deinococcus radiodurans''' | + | {{Structure |
| + | |PDB= 2fbk |SIZE=350|CAPTION= <scene name='initialview01'>2fbk</scene>, resolution 2.300Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''The Crystal Structure of HucR from Deinococcus radiodurans''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2FBK is a [ | + | 2FBK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FBK OCA]. |
==Reference== | ==Reference== | ||
| - | The crystal structure of the transcriptional regulator HucR from Deinococcus radiodurans reveals a repressor preconfigured for DNA binding., Bordelon T, Wilkinson SP, Grove A, Newcomer ME, J Mol Biol. 2006 Jun 30;360(1):168-77. Epub 2006 May 19. PMID:[http:// | + | The crystal structure of the transcriptional regulator HucR from Deinococcus radiodurans reveals a repressor preconfigured for DNA binding., Bordelon T, Wilkinson SP, Grove A, Newcomer ME, J Mol Biol. 2006 Jun 30;360(1):168-77. Epub 2006 May 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16750221 16750221] |
[[Category: Deinococcus radiodurans]] | [[Category: Deinococcus radiodurans]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: winged-helix-turn-helix]] | [[Category: winged-helix-turn-helix]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:50:23 2008'' |
Revision as of 14:50, 20 March 2008
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| , resolution 2.300Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
The Crystal Structure of HucR from Deinococcus radiodurans
Overview
We report here the 2.3 A resolution structure of the hypothetical uricase regulator (HucR) from Deinococcus radiodurans R1. HucR, a member of the MarR family of DNA-binding proteins, was previously shown to repress its own expression as well as that of a uricase, a repression that is alleviated both in vivo and in vitro upon binding uric acid, the substrate for uricase. As uric acid is a potent scavenger of reactive oxygen species, and as D. radiodurans is known for its remarkable resistance to DNA-damaging agents, these observations indicate a novel oxidative stress response mechanism. The crystal structure of HucR in the absence of ligand or DNA reveals a dimer in which the DNA recognition helices are preconfigured for DNA binding. This configuration of DNA-binding domains is achieved through an apparently stable dimer interface that, in contrast to what is observed in other MarR homologs for which structures have been determined, shows little conformational heterogeneity in the absence of ligand. An additional amino-terminal segment, absent from other MarR homologs, appears to brace the principal helix of the dimerization interface. However, although HucR is preconfigured for DNA binding, the presence of a stacked pair of symmetry-related histidine residues at a central pivot point in the dimer interface suggests a mechanism for a conformational change to attenuate DNA binding.
About this Structure
2FBK is a Single protein structure of sequence from Deinococcus radiodurans. Full crystallographic information is available from OCA.
Reference
The crystal structure of the transcriptional regulator HucR from Deinococcus radiodurans reveals a repressor preconfigured for DNA binding., Bordelon T, Wilkinson SP, Grove A, Newcomer ME, J Mol Biol. 2006 Jun 30;360(1):168-77. Epub 2006 May 19. PMID:16750221
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