5VE9

Structure of hACF7 EF1-EF2-GAR domains

  • Classification: PROTEIN BINDING
  • Organism(s): Homo sapiens
  • Expression System: Escherichia coli BL21
  • Mutation(s): No 

  • Deposited: 2017-04-04 Released: 2017-06-21 
  • Deposition Author(s): Lane, T.R., Slep, K.C.
  • Funding Organization(s): National Institutes of Health/Eunice Kennedy Shriver National Institute of Child Health & Human Development (NIH/NICHD), National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS), National Institutes of Health/National Institute of Arthritis and Musculoskeletal and Skin Diseases (NIH/NIAMS)

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.79 Å
  • R-Value Free: 0.279 
  • R-Value Work: 0.256 
  • R-Value Observed: 0.258 

wwPDB Validation   3D Report Full Report


This is version 2.2 of the entry. See complete history


Literature

Structure of the ACF7 EF-Hand-GAR Module and Delineation of Microtubule Binding Determinants.

Lane, T.R.Fuchs, E.Slep, K.C.

(2017) Structure 25: 1130-1138.e6

  • DOI: https://doi.org/10.1016/j.str.2017.05.006
  • Primary Citation of Related Structures:  
    5VE9

  • PubMed Abstract: 

    Spectraplakins are large molecules that cross-link F-actin and microtubules (MTs). Mutations in spectraplakins yield defective cell polarization, aberrant focal adhesion dynamics, and dystonia. We present the 2.8 Å crystal structure of the hACF7 EF1-EF2-GAR MT-binding module and delineate the GAR residues critical for MT binding. The EF1-EF2 and GAR domains are autonomous domains connected by a flexible linker. The EF1-EF2 domain is an EFβ-scaffold with two bound Ca 2+ ions that straddle an N-terminal α helix. The GAR domain has a unique α/β sandwich fold that coordinates Zn 2+ . While the EF1-EF2 domain is not sufficient for MT binding, the GAR domain is and likely enhances EF1-EF2-MT engagement. Residues in a conserved basic patch, distal to the GAR domain's Zn 2+ -binding site, mediate MT binding.


  • Organizational Affiliation

    Department of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, NC 27599, USA; Molecular and Cellular Biophysics Program, University of North Carolina, Chapel Hill, NC 27599, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Microtubule-actin cross-linking factor 1, isoforms 1/2/3/5A,
C [auth B]
91Homo sapiensMutation(s): 0 
Gene Names: MACF1ABP620ACF7KIAA0465KIAA1251
UniProt & NIH Common Fund Data Resources
Find proteins for Q9UPN3 (Homo sapiens)
Explore Q9UPN3 
Go to UniProtKB:  Q9UPN3
PHAROS:  Q9UPN3
GTEx:  ENSG00000127603 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9UPN3
Sequence Annotations
Expand
  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Microtubule-actin cross-linking factor 1, isoforms 1/2/3/5B [auth C]74Homo sapiensMutation(s): 0 
Gene Names: MACF1ABP620ACF7KIAA0465KIAA1251
UniProt & NIH Common Fund Data Resources
Find proteins for Q9UPN3 (Homo sapiens)
Explore Q9UPN3 
Go to UniProtKB:  Q9UPN3
PHAROS:  Q9UPN3
GTEx:  ENSG00000127603 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9UPN3
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.79 Å
  • R-Value Free: 0.279 
  • R-Value Work: 0.256 
  • R-Value Observed: 0.258 
  • Space Group: P 31 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 92.984α = 90
b = 92.984β = 90
c = 90.446γ = 120
Software Package:
Software NamePurpose
PHENIXrefinement
HKL-2000data reduction
HKL-2000data scaling
PHENIXphasing

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
National Institutes of Health/Eunice Kennedy Shriver National Institute of Child Health & Human Development (NIH/NICHD)United StatesR03HD084980
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)United StatesR01GM094415
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)United StatesT32GM008570
National Institutes of Health/National Institute of Arthritis and Musculoskeletal and Skin Diseases (NIH/NIAMS)United StatesR37AR27883

Revision History  (Full details and data files)

  • Version 1.0: 2017-06-21
    Type: Initial release
  • Version 1.1: 2017-07-19
    Changes: Database references
  • Version 1.2: 2017-09-13
    Changes: Author supporting evidence
  • Version 2.0: 2017-11-08
    Changes: Advisory, Atomic model, Database references, Derived calculations
  • Version 2.1: 2019-12-11
    Changes: Author supporting evidence
  • Version 2.2: 2024-03-06
    Changes: Data collection, Database references, Derived calculations