2X31

Modelling of the complex between subunits BchI and BchD of magnesium chelatase based on single-particle cryo-EM reconstruction at 7.5 ang


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 7.50 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

ATP-Induced Conformational Dynamics in the Aaa+ Motor Unit of Magnesium Chelatase.

Lundqvist, J.Elmlund, H.Wulff, R.P.Berglund, L.Elmlund, D.Emanuelsson, C.Hebert, H.Willows, R.D.Hansson, M.Lindahl, M.Al-Karadaghi, S.

(2010) Structure 18: 354

  • DOI: https://doi.org/10.1016/j.str.2010.01.001
  • Primary Citation of Related Structures:  
    2X31

  • PubMed Abstract: 

    Mg-chelatase catalyzes the first committed step of the chlorophyll biosynthetic pathway, the ATP-dependent insertion of Mg(2+) into protoporphyrin IX (PPIX). Here we report the reconstruction using single-particle cryo-electron microscopy of the complex between subunits BchD and BchI of Rhodobacter capsulatus Mg-chelatase in the presence of ADP, the nonhydrolyzable ATP analog AMPPNP, and ATP at 7.5 A, 14 A, and 13 A resolution, respectively. We show that the two AAA+ modules of the subunits form a unique complex of 3 dimers related by a three-fold axis. The reconstructions demonstrate substantial differences between the conformations of the complex in the presence of ATP and ADP, and suggest that the C-terminal integrin-I domains of the BchD subunits play a central role in transmitting conformational changes of BchI to BchD. Based on these data a model for the function of magnesium chelatase is proposed.


  • Organizational Affiliation

    Department of Molecular Biophysics, Centre for Molecular Protein Science, Lund University, Lund, Sweden. joakim@crc.dk


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
MAGNESIUM-CHELATASE 60 KDA SUBUNIT
A, B, C, D, E
A, B, C, D, E, F
189Rhodobacter capsulatusMutation(s): 0 
EC: 6.6.1.1
UniProt
Find proteins for P26175 (Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003))
Explore P26175 
Go to UniProtKB:  P26175
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP26175
Sequence Annotations
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  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
MAGNESIUM-CHELATASE 38 KDA SUBUNIT
G, H, I, J, K
G, H, I, J, K, L
350Rhodobacter capsulatusMutation(s): 0 
EC: 6.6.1.1
UniProt
Find proteins for P26239 (Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003))
Explore P26239 
Go to UniProtKB:  P26239
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP26239
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 7.50 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

Structure Validation

View Full Validation Report



Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2010-11-10
    Type: Initial release
  • Version 1.1: 2012-03-21
    Changes: Other, Version format compliance
  • Version 1.2: 2013-03-20
    Changes: Derived calculations, Refinement description
  • Version 1.3: 2017-04-19
    Changes: Other
  • Version 1.4: 2019-10-23
    Changes: Data collection, Other