PDBsum entry 2bqq

Go to PDB code: 
protein links
Transferase PDB id
Protein chain
96 a.a. *
Waters ×101
* Residue conservation analysis
PDB id:
Name: Transferase
Title: X-ray structure of the n-terminal domain of human doublecort
Structure: Neuronal migration protein doublecortin. Chain: a. Fragment: n-terminal domain residues 45-150. Synonym: doublecortin, lissencephalin-x, lis-x, doublin. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Biol. unit: Dimer (from PDB file)
2.20Å     R-factor:   0.179     R-free:   0.237
Authors: M.H Kim,D.R.Cooper,U.Derewenda,Z.S.Derewenda
Key ref:
T.Cierpicki et al. (2006). The DC-module of doublecortin: dynamics, domain boundaries, and functional implications. Proteins, 64, 874-882. PubMed id: 16835924 DOI: 10.1002/prot.21068
27-Apr-05     Release date:   19-Jul-06    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
O43602  (DCX_HUMAN) -  Neuronal migration protein doublecortin
441 a.a.
96 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     intracellular signal transduction   1 term 


DOI no: 10.1002/prot.21068 Proteins 64:874-882 (2006)
PubMed id: 16835924  
The DC-module of doublecortin: dynamics, domain boundaries, and functional implications.
T.Cierpicki, M.H.Kim, D.R.Cooper, U.Derewenda, J.H.Bushweller, Z.S.Derewenda.
The doublecortin-like (DC) domains, which usually occur in tandem, constitute novel microtubule-binding modules. They were first identified in doublecortin (DCX), a protein expressed in migrating neurons, and in the doublecortin-like kinase (DCLK). They are also found in other proteins, including the RP1 gene product which-when mutated-causes a form of inherited blindness. We previously reported an X-ray structure of the N-terminal DC domain of DCLK (N-DCLK), and a solution structure of an analogous module of human doublecortin (N-DCX). These studies showed that the DC domain has a tertiary fold closely reminiscent of ubiquitin and similar to several GTPase-binding domains. We now report an X-ray structure of a mutant of N-DCX, in which the C-terminal fragment (residues 139-147) unexpectedly shows an altered, "open" conformation. However, heteronuclear NMR data show that this C-terminal fragment is only transiently open in solution, and assumes a predominantly "closed" conformation. While the "open" conformation may be artificially stabilized by crystal packing interactions, the observed switching between the "open" and "closed" conformations, which shortens the linker between the two DC-domains by approximately 20 A, is likely to be of functional importance in the control of tubulin polymerization and microtubule bundling by doublecortin.
  Selected figure(s)  
Figure 1.
Figure 1. Comparison of N-DCX^DD x-ray structure (green) with (A) crystal structure of N-DCLK (magenta) and (B) representative NMR structure of N-DCX (blue). Every tenth residue of N-DCX^DD is numbered and C-terminal Trp residue is shown in sticks.
Figure 2.
Figure 2. Crystal contacts around K134D/K135D. A: Four crystallographically related monomers of N-DCX^DD are shown with residues 134 and 135 shown as magenta spheres. While Asp135 does not directly participate in any crystallographic contacts, Asp135 participates in two types of crystal contacts. B: Stereoview of the crystal contacts of the C-terminal fragment looking approximately down the crystallographic twofold. Key residues are labeled and intramolecular hydrogen bonds are shown.
  The above figures are reprinted by permission from John Wiley & Sons, Inc.: Proteins (2006, 64, 874-882) copyright 2006.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21046408 G.Friocourt, P.Marcorelles, P.Saugier-Veber, M.L.Quille, S.Marret, and A.Laquerrière (2011).
Role of cytoskeletal abnormalities in the neuropathology and pathophysiology of type I lissencephaly.
  Acta Neuropathol, 121, 149-170.  
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.