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PDBsum entry 3k1l

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protein ligands metals Protein-protein interface(s) links
Ligase PDB id
3k1l
Jmol
Contents
Protein chains
364 a.a. *
Ligands
MAL ×2
CIT ×3
Metals
_AU ×13
_ZN ×4
Waters ×13
* Residue conservation analysis
PDB id:
3k1l
Name: Ligase
Title: Crystal structure of fancl
Structure: Fancl. Chain: b, a. Synonym: at07283p, e3 ligase. Engineered: yes
Source: Drosophila melanogaster. Fruit fly. Organism_taxid: 7227. Gene: cg12812. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
3.20Å     R-factor:   0.207     R-free:   0.247
Authors: A.R.Cole,H.Walden
Key ref: A.R.Cole et al. (2010). The structure of the catalytic subunit FANCL of the Fanconi anemia core complex. Nat Struct Mol Biol, 17, 294-298. PubMed id: 20154706
Date:
28-Sep-09     Release date:   16-Feb-10    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q8T913  (Q8T913_DROME) -  AT07283p
Seq:
Struc:
381 a.a.
364 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cellular_component   2 terms 
  Biological process     DNA repair   2 terms 
  Biochemical function     metal ion binding     2 terms  

 

 
Nat Struct Mol Biol 17:294-298 (2010)
PubMed id: 20154706  
 
 
The structure of the catalytic subunit FANCL of the Fanconi anemia core complex.
A.R.Cole, L.P.Lewis, H.Walden.
 
  ABSTRACT  
 
The Fanconi anemia (FA) pathway is activated in response to DNA damage, leading to monoubiquitination of the substrates FANCI and FANCD2 by the FA core complex. Here we report the crystal structure of FANCL, the catalytic subunit of the FA core complex, at 3.2 A. The structure reveals an architecture fundamentally different from previous sequence-based predictions. The molecule is composed of an N-terminal E2-like fold, which we term the ELF domain, a novel double-RWD (DRWD) domain, and a C-terminal really interesting new gene (RING) domain predicted to facilitate E2 binding. Binding assays show that the DRWD domain, but not the ELF domain, is responsible for substrate binding.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20730555 A.Guainazzi, and O.D.Schärer (2010).
Using synthetic DNA interstrand crosslinks to elucidate repair pathways and identify new therapeutic targets for cancer chemotherapy.
  Cell Mol Life Sci, 67, 3683-3697.  
20603073 A.Smogorzewska, R.Desetty, T.T.Saito, M.Schlabach, F.P.Lach, M.E.Sowa, A.B.Clark, T.A.Kunkel, J.W.Harper, M.P.Colaiácovo, and S.J.Elledge (2010).
A genetic screen identifies FAN1, a Fanconi anemia-associated nuclease necessary for DNA interstrand crosslink repair.
  Mol Cell, 39, 36-47.  
20551964 H.D.Ulrich, and H.Walden (2010).
Ubiquitin signalling in DNA replication and repair.
  Nat Rev Mol Cell Biol, 11, 479-489.  
20937699 L.Geng, C.J.Huntoon, and L.M.Karnitz (2010).
RAD18-mediated ubiquitination of PCNA activates the Fanconi anemia DNA repair network.
  J Cell Biol, 191, 249-257.  
20670886 L.O'Donnell, and D.Durocher (2010).
DNA repair has a new FAN1 club.
  Mol Cell, 39, 167-169.  
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.