4JJ0

Crystal structure of MamP


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.80 Å
  • R-Value Free: 0.239 
  • R-Value Work: 0.182 
  • R-Value Observed: 0.183 

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Ligand Structure Quality Assessment 


This is version 1.1 of the entry. See complete history


Literature

Structural insight into magnetochrome-mediated magnetite biomineralization.

Siponen, M.I.Legrand, P.Widdrat, M.Jones, S.R.Zhang, W.J.Chang, M.C.Faivre, D.Arnoux, P.Pignol, D.

(2013) Nature 502: 681-684

  • DOI: https://doi.org/10.1038/nature12573
  • Primary Citation of Related Structures:  
    4JJ0, 4JJ3

  • PubMed Abstract: 

    Magnetotactic bacteria align along the Earth's magnetic field using an organelle called the magnetosome, a biomineralized magnetite (Fe(II)Fe(III)2O4) or greigite (Fe(II)Fe(III)2S4) crystal embedded in a lipid vesicle. Although the need for both iron(II) and iron(III) is clear, little is known about the biological mechanisms controlling their ratio. Here we present the structure of the magnetosome-associated protein MamP and find that it is built on a unique arrangement of a self-plugged PDZ domain fused to two magnetochrome domains, defining a new class of c-type cytochrome exclusively found in magnetotactic bacteria. Mutational analysis, enzyme kinetics, co-crystallization with iron(II) and an in vitro MamP-assisted magnetite production assay establish MamP as an iron oxidase that contributes to the formation of iron(III) ferrihydrite eventually required for magnetite crystal growth in vivo. These results demonstrate the molecular mechanisms of iron management taking place inside the magnetosome and highlight the role of magnetochrome in iron biomineralization.


  • Organizational Affiliation

    1] Commissariat à l'Energie Atomique et aux Energies Alternatives, Direction des Sciences du Vivant, Institut de Biologie Environnementale et de Biotechnologies,, F-13108, France [2] Centre National de la Recherche Scientifique, Unité Mixte de Recherche Biologie Végétale et Microbiologie Environnementales, Saint-Paul-lez-Durance, F-13108, France [3] Aix-Marseille Université, Saint-Paul-lez-Durance, F-13108, France.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
MamP
A, B
243Magnetococcus marinus MC-1Mutation(s): 0 
UniProt
Find proteins for A0L9W2 (Magnetococcus marinus (strain ATCC BAA-1437 / JCM 17883 / MC-1))
Explore A0L9W2 
Go to UniProtKB:  A0L9W2
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0L9W2
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.80 Å
  • R-Value Free: 0.239 
  • R-Value Work: 0.182 
  • R-Value Observed: 0.183 
  • Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 81.24α = 90
b = 95.81β = 115.33
c = 54.32γ = 90
Software Package:
Software NamePurpose
DNAdata collection
SHARPphasing
REFMACrefinement
MOSFLMdata reduction
SCALAdata scaling

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2013-10-09
    Type: Initial release
  • Version 1.1: 2013-11-13
    Changes: Database references