1T5C

Crystal structure of the motor domain of human kinetochore protein CENP-E


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.50 Å
  • R-Value Free: 0.278 
  • R-Value Work: 0.228 

wwPDB Validation   3D Report Full Report


This is version 2.1 of the entry. See complete history


Literature

Crystal structure of the motor domain of the human kinetochore protein CENP-E.

Garcia-Saez, I.Yen, T.Wade, R.H.Kozielski, F.

(2004) J Mol Biol 340: 1107-1116

  • DOI: https://doi.org/10.1016/j.jmb.2004.05.053
  • Primary Citation of Related Structures:  
    1T5C

  • PubMed Abstract: 

    The human kinetochore is a highly complex macromolecular structure that connects chromosomes to spindle microtubules (MTs) in order to facilitate accurate chromosome segregation. Centromere-associated protein E (CENP-E), a member of the kinesin superfamily, is an essential component of the kinetochore, since it is required to stabilize the attachment of chromosomes to spindle MTs, to develop tension across aligned chromosomes, to stabilize spindle poles and to satisfy the mitotic checkpoint. Here we report the 2.5A resolution crystal structure of the motor domain and linker region of human CENP-E with MgADP bound in the active site. This structure displays subtle but important differences compared to the structures of human Eg5 and conventional kinesin. Our structure reveals that the CENP-E linker region is in a "docked" position identical to that in the human plus-end directed conventional kinesin. CENP-E has many advantages as a potential anti-mitotic drug target and this crystal structure of human CENP-E will provide a starting point for high throughput virtual screening of potential inhibitors.


  • Organizational Affiliation

    Laboratoire de Microscopie Electronique Structurale, Institut de Biologie Structurale, 41 rue Jules Horowitz, 38027 Grenoble Cedex 01, France.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Centromeric protein E
A, B
349Homo sapiensMutation(s): 0 
Gene Names: CENPE
UniProt & NIH Common Fund Data Resources
Find proteins for Q02224 (Homo sapiens)
Explore Q02224 
Go to UniProtKB:  Q02224
PHAROS:  Q02224
GTEx:  ENSG00000138778 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ02224
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 4 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
ADP
Query on ADP

Download Ideal Coordinates CCD File 
E [auth A],
H [auth B]
ADENOSINE-5'-DIPHOSPHATE
C10 H15 N5 O10 P2
XTWYTFMLZFPYCI-KQYNXXCUSA-N
PIN
Query on PIN

Download Ideal Coordinates CCD File 
F [auth A]PIPERAZINE-N,N'-BIS(2-ETHANESULFONIC ACID)
C8 H18 N2 O6 S2
IHPYMWDTONKSCO-UHFFFAOYSA-N
NO3
Query on NO3

Download Ideal Coordinates CCD File 
D [auth A]NITRATE ION
N O3
NHNBFGGVMKEFGY-UHFFFAOYSA-N
MG
Query on MG

Download Ideal Coordinates CCD File 
C [auth A],
G [auth B]
MAGNESIUM ION
Mg
JLVVSXFLKOJNIY-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.50 Å
  • R-Value Free: 0.278 
  • R-Value Work: 0.228 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 49.353α = 90
b = 83.7β = 103.05
c = 94.162γ = 90
Software Package:
Software NamePurpose
DENZOdata reduction
SCALAdata scaling
AMoREphasing
CNSrefinement
CCP4data scaling

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2005-05-10
    Type: Initial release
  • Version 1.1: 2008-04-30
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 2.0: 2020-06-17
    Changes: Advisory, Database references, Polymer sequence
  • Version 2.1: 2023-08-23
    Changes: Advisory, Data collection, Database references, Derived calculations, Refinement description