1RHW

The solution structure of the pH-induced monomer of dynein light chain LC8 from Drosophila


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 56 
  • Conformers Submitted: 10 
  • Selection Criteria: target function 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

The solution structure of the pH-induced monomer of dynein light-chain LC8 from Drosophila.

Makokha, M.Huang, Y.J.Montelione, G.Edison, A.S.Barbar, E.

(2004) Protein Sci 13: 727-734

  • DOI: https://doi.org/10.1110/ps.03462204
  • Primary Citation of Related Structures:  
    1RHW

  • PubMed Abstract: 

    The structure of Drosophila LC8 pH-induced monomer has been determined by NMR spectroscopy using the program AutoStructure. The structure at pH 3 and 30 degrees C is similar to the individual subunits of mammalian LC8 dimer with the exception that a beta strand, which crosses between monomers to form an intersubunit beta-sheet in the dimer, is a flexible loop with turnlike conformations in the monomer. Increased flexibility in the interface region relative to the rest of the protein is confirmed by dynamic measurements based on (15)N relaxation. Comparison of the monomer and dimer structures indicates that LC8 is not a domain swapped dimer.


  • Organizational Affiliation

    Department of Biochemistry and Biophysics, Ohio University, Athens, 45701-2979, USA.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Dynein light chain 1, cytoplasmic89Drosophila melanogasterMutation(s): 0 
Gene Names: CTPCDLC1DDLC1CG6998
UniProt
Find proteins for Q24117 (Drosophila melanogaster)
Explore Q24117 
Go to UniProtKB:  Q24117
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ24117
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 56 
  • Conformers Submitted: 10 
  • Selection Criteria: target function 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2004-04-27
    Type: Initial release
  • Version 1.1: 2008-04-29
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2022-03-02
    Changes: Data collection, Database references, Derived calculations