1TOV

Structural genomics of Caenorhabditis elegans: CAP-GLY domain of F53F4.3


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.77 Å
  • R-Value Free: 0.259 
  • R-Value Work: 0.211 
  • R-Value Observed: 0.213 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Crystal Structure of the Cytoskeleton-Associated Protein Glycine-Rich (CAP-Gly) Domain

Li, S.Finley, J.Liu, Z.J.Qiu, S.H.Luan, C.H.Carson, M.Tsao, J.Johnson, D.Lin, G.Zhao, J.Thomas, W.Nagy, L.A.Sha, B.Delucas, L.J.Wang, B.C.Luo, M.

(2002) J Biol Chem 277: 48596-48601

  • DOI: https://doi.org/10.1074/jbc.M208512200
  • Primary Citation of Related Structures:  
    1LPL, 1TOV

  • PubMed Abstract: 

    Cytoskeleton-associated proteins (CAPs) are involved in the organization of microtubules and transportation of vesicles and organelles along the cytoskeletal network. A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of the CAP-Gly domain of Caenorhabditis elegans F53F4.3 protein, solved by single wavelength sulfur-anomalous phasing, revealed a novel protein fold containing three beta-sheets. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove. Residues in the groove are highly conserved as measured from the information content of the aligned sequences. The C-terminal tail of another molecule in the crystal is bound in this groove.


  • Organizational Affiliation

    Southeast Collaboratory for Structural Genomics, University of Georgia, Athens 30602, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Hypothetical protein F53F4.3 in chromosome V98Caenorhabditis elegansMutation(s): 0 
Gene Names: F53F4.3
UniProt
Find proteins for Q20728 (Caenorhabditis elegans)
Explore Q20728 
Go to UniProtKB:  Q20728
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ20728
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
SO4
Query on SO4

Download Ideal Coordinates CCD File 
B [auth A]SULFATE ION
O4 S
QAOWNCQODCNURD-UHFFFAOYSA-L
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.77 Å
  • R-Value Free: 0.259 
  • R-Value Work: 0.211 
  • R-Value Observed: 0.213 
  • Space Group: P 61 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 64.156α = 90
b = 64.156β = 90
c = 101.946γ = 120
Software Package:
Software NamePurpose
HKL-2000data collection
HKL-2000data reduction
ISAS2001model building
REFMACrefinement
HKL-2000data scaling
ISASphasing

Structure Validation

View Full Validation Report



Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2004-07-27
    Type: Initial release
  • Version 1.1: 2008-04-30
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2024-02-14
    Changes: Data collection, Database references, Derived calculations