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PDBsum entry 2v0e

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Hydrolase PDB id
2v0e

 

 

 

 

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Contents
Protein chain
55 a.a. *
* Residue conservation analysis
PDB id:
2v0e
Name: Hydrolase
Title: Brk domain from human chd7
Structure: Chromodomain-helicase-DNA-binding protein 7. Chain: a. Fragment: brk domain, residues 1799-1852. Synonym: atp- dependent helicase chd7, chd-7. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Expression_system_variant: c41.
NMR struc: 20 models
Authors: M.D.Allen,T.L.Religa,S.M.V.Freund,M.Bycroft
Key ref:
M.D.Allen et al. (2007). Solution structure of the BRK domains from CHD7. J Mol Biol, 371, 1135-1140. PubMed id: 17603073 DOI: 10.1016/j.jmb.2007.06.007
Date:
14-May-07     Release date:   22-May-07    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q9P2D1  (CHD7_HUMAN) -  Chromodomain-helicase-DNA-binding protein 7 from Homo sapiens
Seq:
Struc:
 
Seq:
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Seq:
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Seq:
Struc:
2997 a.a.
55 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.3.6.4.12  - Dna helicase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + H2O = ADP + phosphate + H+
ATP
+ H2O
= ADP
+ phosphate
+ H(+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
DOI no: 10.1016/j.jmb.2007.06.007 J Mol Biol 371:1135-1140 (2007)
PubMed id: 17603073  
 
 
Solution structure of the BRK domains from CHD7.
M.D.Allen, T.L.Religa, S.M.Freund, M.Bycroft.
 
  ABSTRACT  
 
CHD7 is a member of the chromodomain helicase DNA binding domain (CHD) family of ATP-dependent chromatin remodelling enzymes. It is mutated in CHARGE syndrome, a multiple congenital anomaly condition. CHD7 is one of a subset of CHD proteins, unique to metazoans that contain the BRK domain, a protein module also found in the Brahma/BRG1 family of helicases. We describe here the NMR solution structure of the two BRK domains of CHD7. Each domain has a compact betabetaalphabeta fold. The second domain has a C-terminal extension consisting of two additional helices. The structure differs from those of other domains present in chromatin-associated proteins.
 
  Selected figure(s)  
 
Figure 3.
Figure 3. CTCF binding. A GST fusion protein of the zinc finger domains of human CTCF (lane 3) bound to glutathione beads was incubated with the BRK domains of CHD7. After repeated washing steps, binding of the BRK domains was analysed by SDS–PAGE followed by Coomassie staining of the gel (lane 4). GST served as a negative control (lanes 5 and 6). For comparison, the BRK input is shown in lane 1. The BRK domains did not bind to glutathione beads (lane 2).
 
  The above figure is reprinted by permission from Elsevier: J Mol Biol (2007, 371, 1135-1140) copyright 2007.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20716578 D.J.Melicharek, L.C.Ramirez, S.Singh, R.Thompson, and D.R.Marenda (2010).
Kismet/CHD7 regulates axon morphology, memory and locomotion in a Drosophila model of CHARGE syndrome.
  Hum Mol Genet, 19, 4253-4264.  
20111866 M.J.Lathrop, L.Chakrabarti, J.Eng, C.H.Rhodes, T.Lutz, A.Nieto, H.D.Liggitt, S.Warner, J.Fields, R.Stöger, and S.Fiering (2010).
Deletion of the Chd6 exon 12 affects motor coordination.
  Mamm Genome, 21, 130-142.  
20148317 S.V.Saladi, and I.L.de la Serna (2010).
ATP dependent chromatin remodeling enzymes in embryonic stem cells.
  Stem Cell Rev, 6, 62-73.  
  18301784 K.W.Trotter, and T.K.Archer (2008).
The BRG1 transcriptional coregulator.
  Nucl Recept Signal, 6, e004.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.

 

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