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PDBsum entry 4k0r

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protein links
Circadian clock protein PDB id
4k0r

 

 

 

 

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Contents
Protein chain
463 a.a.
Waters ×71
PDB id:
4k0r
Name: Circadian clock protein
Title: Crystal structure of mouse cryptochrome 1
Structure: Cryptochrome-1. Chain: a. Engineered: yes
Source: Mus musculus. Mouse. Organism_taxid: 10090. Gene: cry1. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108
Resolution:
2.65Å     R-factor:   0.194     R-free:   0.260
Authors: A.Czarna,E.Wolf
Key ref: A.Czarna et al. (2013). Structures of Drosophila cryptochrome and mouse cryptochrome1 provide insight into circadian function. Cell, 153, 1394-1405. PubMed id: 23746849 DOI: 10.1016/j.cell.2013.05.011
Date:
04-Apr-13     Release date:   26-Jun-13    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P97784  (CRY1_MOUSE) -  Cryptochrome-1 from Mus musculus
Seq:
Struc:
 
Seq:
Struc:
606 a.a.
463 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
DOI no: 10.1016/j.cell.2013.05.011 Cell 153:1394-1405 (2013)
PubMed id: 23746849  
 
 
Structures of Drosophila cryptochrome and mouse cryptochrome1 provide insight into circadian function.
A.Czarna, A.Berndt, H.R.Singh, A.Grudziecki, A.G.Ladurner, G.Timinszky, A.Kramer, E.Wolf.
 
  ABSTRACT  
 
Drosophila cryptochrome (dCRY) is a FAD-dependent circadian photoreceptor, whereas mammalian cryptochromes (CRY1/2) are integral clock components that repress mCLOCK/mBMAL1-dependent transcription. We report crystal structures of full-length dCRY, a dCRY loop deletion construct, and the photolyase homology region of mouse CRY1 (mCRY1). Our dCRY structures depict Phe534 of the regulatory tail in the same location as the photolesion in DNA-repairing photolyases and reveal that the sulfur loop and tail residue Cys523 plays key roles in the dCRY photoreaction. Our mCRY1 structure visualizes previously characterized mutations, an NLS, and MAPK and AMPK phosphorylation sites. We show that the FAD and antenna chromophore-binding regions, a predicted coiled-coil helix, the C-terminal lid, and charged surfaces are involved in FAD-independent mPER2 and FBXL3 binding and mCLOCK/mBMAL1 transcriptional repression. The structure of a mammalian cryptochrome1 protein may catalyze the development of CRY chemical probes and the design of therapeutic metabolic modulators.
 

 

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