2N88

Chromodomain 3 (CD3) of cpSRP43


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 20 
  • Conformers Submitted: 
  • Selection Criteria: structures with the least restraint violations 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

Structural basis for cpSRP43 chromodomain selectivity and dynamics in Alb3 insertase interaction.

Horn, A.Hennig, J.Ahmed, Y.L.Stier, G.Wild, K.Sattler, M.Sinning, I.

(2015) Nat Commun 6: 8875-8875

  • DOI: https://doi.org/10.1038/ncomms9875
  • Primary Citation of Related Structures:  
    2N88, 5E4W, 5E4X

  • PubMed Abstract: 

    Canonical membrane protein biogenesis requires co-translational delivery of ribosome-associated proteins to the Sec translocase and depends on the signal recognition particle (SRP) and its receptor (SR). In contrast, high-throughput delivery of abundant light-harvesting chlorophyll a,b-binding proteins (LHCPs) in chloroplasts to the Alb3 insertase occurs post-translationally via a soluble transit complex including the cpSRP43/cpSRP54 heterodimer (cpSRP). Here we describe the molecular mechanisms of tethering cpSRP to the Alb3 insertase by specific interaction of cpSRP43 chromodomain 3 with a linear motif in the Alb3 C-terminal tail. Combining NMR spectroscopy, X-ray crystallography and biochemical analyses, we dissect the structural basis for selectivity of chromodomains 2 and 3 for their respective ligands cpSRP54 and Alb3, respectively. Negative cooperativity in ligand binding can be explained by dynamics in the chromodomain interface. Our study provides a model for membrane recruitment of the transit complex and may serve as a prototype for a functional gain by the tandem arrangement of chromodomains.


  • Organizational Affiliation

    Heidelberg University Biochemistry Center (BZH), INF 328, Heidelberg D-69120, Germany.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Signal recognition particle 43 kDa protein, chloroplastic58Arabidopsis thalianaMutation(s): 0 
Gene Names: CAOCPSRP43At2g47450T30B22.25
UniProt
Find proteins for O22265 (Arabidopsis thaliana)
Explore O22265 
Go to UniProtKB:  O22265
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupO22265
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 20 
  • Conformers Submitted: 
  • Selection Criteria: structures with the least restraint violations 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2015-12-09
    Type: Initial release
  • Version 1.1: 2023-06-14
    Changes: Data collection, Database references, Other