2A10

carboxysome shell protein ccmK4


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.80 Å
  • R-Value Free: 0.227 
  • R-Value Work: 0.193 
  • R-Value Observed: 0.194 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

Protein structures forming the shell of primitive bacterial organelles

Kerfeld, C.A.Sawaya, M.R.Tanaka, S.Nguyen, C.V.Phillips, M.Beeby, M.Yeates, T.O.

(2005) Science 309: 936-938

  • DOI: https://doi.org/10.1126/science.1113397
  • Primary Citation of Related Structures:  
    2A10, 2A18, 2A1B

  • PubMed Abstract: 

    Bacterial microcompartments are primitive organelles composed entirely of protein subunits. Genomic sequence databases reveal the widespread occurrence of microcompartments across diverse microbes. The prototypical bacterial microcompartment is the carboxysome, a protein shell for sequestering carbon fixation reactions. We report three-dimensional crystal structures of multiple carboxysome shell proteins, revealing a hexameric unit as the basic microcompartment building block and showing how these hexamers assemble to form flat facets of the polyhedral shell. The structures suggest how molecular transport across the shell may be controlled and how structural variations might govern the assembly and architecture of these subcellular compartments.


  • Organizational Affiliation

    Molecular Biology Institute, University of California, Los Angeles (UCLA), Box 951570, Los Angeles, CA 90095, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Carbon dioxide concentrating mechanism protein ccmK homolog 4
A, B, C, D, E
A, B, C, D, E, F
125Synechocystis sp. PCC 6803Mutation(s): 0 
Gene Names: ccmK4
UniProt
Find proteins for P73407 (Synechocystis sp. (strain PCC 6803 / Kazusa))
Explore P73407 
Go to UniProtKB:  P73407
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP73407
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.80 Å
  • R-Value Free: 0.227 
  • R-Value Work: 0.193 
  • R-Value Observed: 0.194 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 84.758α = 90
b = 87β = 90
c = 96.512γ = 90
Software Package:
Software NamePurpose
Blu-Icedata collection
SCALEPACKdata scaling
MLPHAREphasing
REFMACrefinement

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2005-08-09
    Type: Initial release
  • Version 1.1: 2008-04-30
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Advisory, Source and taxonomy, Version format compliance
  • Version 1.3: 2017-10-11
    Changes: Refinement description
  • Version 1.4: 2024-02-14
    Changes: Data collection, Database references, Derived calculations