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PDBsum entry 4jj0

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protein ligands Protein-protein interface(s) links
Electron transport PDB id
4jj0

 

 

 

 

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Contents
Protein chains
181 a.a.
Ligands
HEC ×4
GOL
Waters ×336
PDB id:
4jj0
Name: Electron transport
Title: Crystal structure of mamp
Structure: Mamp. Chain: a, b. Fragment: unp residues 26-268. Engineered: yes
Source: Magnetococcus. Organism_taxid: 156889. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
1.80Å     R-factor:   0.183     R-free:   0.239
Authors: M.Siponen,D.Pignol,P.Arnoux
Key ref: M.I.Siponen et al. (2013). Structural insight into magnetochrome-mediated magnetite biomineralization. Nature, 502, 681-684. PubMed id: 24097349 DOI: 10.1038/nature12573
Date:
07-Mar-13     Release date:   09-Oct-13    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
A0L9W2  (A0L9W2_MAGMM) -  PDZ/DHR/GLGF domain protein from Magnetococcus marinus (strain ATCC BAA-1437 / JCM 17883 / MC-1)
Seq:
Struc:
261 a.a.
181 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 19 residue positions (black crosses)

 

 
DOI no: 10.1038/nature12573 Nature 502:681-684 (2013)
PubMed id: 24097349  
 
 
Structural insight into magnetochrome-mediated magnetite biomineralization.
M.I.Siponen, P.Legrand, M.Widdrat, S.R.Jones, W.J.Zhang, M.C.Chang, D.Faivre, P.Arnoux, D.Pignol.
 
  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.
 

 

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