Structural insight into magnetochrome-mediated magnetite biomineralization
The magnetosome-associated protein mamP is an iron oxidase that reveals 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. Structure of magnetosome protein MamP Magnetotactic ba...
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Veröffentlicht in: | Nature (London) 2013-10, Vol.502 (7473), p.681-684 |
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Sprache: | eng |
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Zusammenfassung: | The magnetosome-associated protein mamP is an iron oxidase that reveals 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.
Structure of magnetosome protein MamP
Magnetotactic bacteria use a specialized organelle known as the magnetosome, a biomineralized crystal of magnetite (Fe(
II
)Fe(
III
)
2
O
4
) or greigite (Fe(
II
)Fe(
III
)
2
S
4
), to sense and align along the Earth's magnetic field. This paper presents the X-ray crystal structure of the magnetosome-associated protein MamP, revealing a unique arrangement of a self-plugged PDZ domain fused to two magnetochrome domains. The authors also establish that MamP is an iron oxidase that contributes to the formation of iron(
III
) ferrihydrite, and is therefore important for mechanisms of iron management during magnetosome biogenesis.
Magnetotactic bacteria align along the Earth’s magnetic field using an organelle called the magnetosome, a biomineralized magnetite (Fe(
ii
)Fe(
iii
)
2
O
4
) or greigite (Fe(
ii
)Fe(
iii
)
2
S
4
) 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
1
. 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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ISSN: | 0028-0836 1476-4687 |
DOI: | 10.1038/nature12573 |