PDBsum entry 2htf

Go to PDB code: 
protein links
Transferase PDB id
Protein chain
105 a.a. *
* Residue conservation analysis
PDB id:
Name: Transferase
Title: The solution structure of the brct domain from human polymerase reveals homology with the tdt brct domain
Structure: DNA polymerase mu. Chain: a. Fragment: brct domain. Synonym: pol mu. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: polm. Expressed in: escherichia coli. Expression_system_taxid: 562
NMR struc: 11 models
Authors: E.F.Derose,M.W.Clarkson,S.A.Gilmore,D.A.Ramsden,G.A.Mueller, R.E.London,A.L.Lee
Key ref: E.F.DeRose et al. (2007). Solution structure of polymerase mu's BRCT Domain reveals an element essential for its role in nonhomologous end joining. Biochemistry, 46, 12100-12110. PubMed id: 17915942
25-Jul-06     Release date:   27-Feb-07    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
Q9NP87  (DPOLM_HUMAN) -  DNA-directed DNA/RNA polymerase mu
494 a.a.
105 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.  - DNA-directed Dna polymerase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
Deoxynucleoside triphosphate
+ DNA(n)
= diphosphate
+ DNA(n+1)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biochemical function     DNA polymerase activity     1 term  


Biochemistry 46:12100-12110 (2007)
PubMed id: 17915942  
Solution structure of polymerase mu's BRCT Domain reveals an element essential for its role in nonhomologous end joining.
E.F.DeRose, M.W.Clarkson, S.A.Gilmore, C.J.Galban, A.Tripathy, J.M.Havener, G.A.Mueller, D.A.Ramsden, R.E.London, A.L.Lee.
The solution structure and dynamics of the BRCT domain from human DNA polymerase mu, implicated in repair of chromosome breaks by nonhomologous end joining (NHEJ), has been determined using NMR methods. BRCT domains are typically involved in protein-protein interactions between factors required for the cellular response to DNA damage. The pol mu BRCT domain is atypical in that, unlike other reported BRCT structures, the pol mu BRCT is neither part of a tandem grouping, nor does it appear to form stable homodimers. Although the sequence of the pol mu BRCT domain has some unique characteristics, particularly the presence of >10% proline residues, it forms the characteristic alphabetaalpha sandwich, in which three alpha helices are arrayed around a central four-stranded beta-sheet. The structure of helix alpha1 is characterized by two solvent-exposed hydrophobic residues, F46 and L50, suggesting that this element may play a role in mediating interactions of pol mu with other proteins. Consistent with this argument, mutation of these residues, as well as the proximal, conserved residue R43, specifically blocked the ability of pol mu to efficiently work together with NHEJ factors Ku and XRCC4-ligase IV to join noncomplementary ends together in vitro. The structural, dynamic, and biochemical evidence reported here identifies a functional surface in the pol mu BRCT domain critical for promoting assembly and activity of the NHEJ machinery. Further, the similarity between the interaction regions of the BRCT domains of pol mu and TdT support the conclusion that they participate in NHEJ as alternate polymerases.

Literature references that cite this PDB file's key reference

  PubMed id Reference
18582474 C.Xu, L.Wu, G.Cui, M.V.Botuyan, J.Chen, and G.Mer (2008).
Structure of a second BRCT domain identified in the nijmegen breakage syndrome protein Nbs1 and its function in an MDC1-dependent localization of Nbs1 to DNA damage sites.
  J Mol Biol, 381, 361-372.
PDB code: 2k2w
18585102 G.A.Mueller, A.F.Moon, E.F.Derose, J.M.Havener, D.A.Ramsden, L.C.Pedersen, and R.E.London (2008).
A comparison of BRCT domains involved in nonhomologous end-joining: introducing the solution structure of the BRCT domain of polymerase lambda.
  DNA Repair (Amst), 7, 1340-1351.  
18215308 K.A.Henry, and F.P.Boscoe (2008).
Estimating the accuracy of geographical imputation.
  Int J Health Geogr, 7, 3.  
18558713 R.Kusumoto, L.Dawut, C.Marchetti, J.Wan Lee, A.Vindigni, D.Ramsden, and V.A.Bohr (2008).
Werner protein cooperates with the XRCC4-DNA ligase IV complex in end-processing.
  Biochemistry, 47, 7548-7556.  
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. Where a reference describes a PDB structure, the PDB code is shown on the right.