6BRS

The Crystal Structure of the Ferredoxin Protease FusC in complex with Arabidopsis Ferredoxin, Ethylmercury phosphate soaked dataset

Summary for 6BRS

• Entry DOI: 10.2210/pdb6brs/pdb
• Descriptor: Putative zinc protease, Ferredoxin-2, chloroplastic, unidentified Ferredoxin peptide, ... (6 entities in total)
• Functional Keywords: m16 protease, ferredoxin binding, ferredoxin cleavage, hydrolase
• Biological source: Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia carotovora subsp. atroseptica); More
• Total number of polymer chains: 4
• Total formula weight: 125709.68

Authors

Grinter, R. (deposition date: 2017-11-30, release date: 2018-06-20, Last modification date: 2024-03-13)

Primary citation

Grinter, R.,Hay, I.D.,Song, J.,Wang, J.,Teng, D.,Dhanesakaran, V.,Wilksch, J.J.,Davies, M.R.,Littler, D.,Beckham, S.A.,Henderson, I.R.,Strugnell, R.A.,Dougan, G.,Lithgow, T.
FusC, a member of the M16 protease family acquired by bacteria for iron piracy against plants.
PLoS Biol., 16:e2006026-e2006026, 2018

PubMed Abstract: Iron is essential for life. Accessing iron from the environment can be a limiting factor that determines success in a given environmental niche. For bacteria, access of chelated iron from the environment is often mediated by TonB-dependent transporters (TBDTs), which are β-barrel proteins that form sophisticated channels in the outer membrane. Reports of iron-bearing proteins being used as a source of iron indicate specific protein import reactions across the bacterial outer membrane. The molecular mechanism by which a folded protein can be imported in this way had remained mysterious, as did the evolutionary process that could lead to such a protein import pathway. How does the bacterium evolve the specificity factors that would be required to select and import a protein encoded on another organism's genome? We describe here a model whereby the plant iron-bearing protein ferredoxin can be imported across the outer membrane of the plant pathogen Pectobacterium by means of a Brownian ratchet mechanism, thereby liberating iron into the bacterium to enable its growth in plant tissues. This import pathway is facilitated by FusC, a member of the same protein family as the mitochondrial processing peptidase (MPP). The Brownian ratchet depends on binding sites discovered in crystal structures of FusC that engage a linear segment of the plant protein ferredoxin. Sequence relationships suggest that the bacterial gene encoding FusC has previously unappreciated homologues in plants and that the protein import mechanism employed by the bacterium is an evolutionary echo of the protein import pathway in plant mitochondria and plastids.

PubMed: 30071011
DOI: 10.1371/journal.pbio.2006026

Experimental method

X-RAY DIFFRACTION (2.3 Å)