Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	FusC, a member of the M16 protease family acquired by bacteria for iron piracy against plants.
Journal, issue, pages	PLoS Biol, Vol. 16, Issue 8, Page e2006026, Year 2018
Publish date	Aug 2, 2018
Authors	Rhys Grinter / Iain D Hay / Jiangning Song / Jiawei Wang / Don Teng / Vijay Dhanesakaran / Jonathan J Wilksch / Mark R Davies / Dene Littler / Simone A Beckham / Ian R Henderson / Richard A Strugnell / Gordon Dougan / Trevor Lithgow /
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 ...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.
External links	PLoS Biol / PubMed:30071011 / PubMed Central
Methods	SAS (X-ray synchrotron) / X-ray diffraction
Resolution	1.9 - 2.7 Å
Structure data	SASDD27: The ferredoxin protease, FusC, E83A mutant + 50 µM Arabidopsis ferredoxin Method: SAXS/SANS SASDD37: The ferredoxin protease, FusC, E83A mutant + 70 µM Arabidopsis ferredoxin Method: SAXS/SANS SASDD47: The ferredoxin protease, FusC, E83A mutant + 100 µM Arabidopsis ferredoxin Method: SAXS/SANS SASDD57: The ferredoxin protease, FusC, E83A mutant + 150 µM Arabidopsis ferredoxin Method: SAXS/SANS SASDD67: The ferredoxin protease, FusC, E83A mutant + 200 µM Arabidopsis ferredoxin Method: SAXS/SANS SASDD77: The ferredoxin protease, FusC, E83A mutant + 300 µM Arabidopsis ferredoxin Method: SAXS/SANS SASDDQ6: The ferredoxin protease, FusC (Ferredoxin Protease, FusC) Method: SAXS/SANS SASDDR6: The ferredoxin protease, FusC, E83A mutant (Ferredoxin protease E83A mutant, FusC E83A) Method: SAXS/SANS SASDDS6: The ferredoxin protease, FusC, with Arabidopsis ferredoxin (co-SEC-SAXS) Method: SAXS/SANS SASDDT6: The ferredoxin protease, FusC, E83A mutant with Arabidopsis ferredoxin (co-SEC-SAXS) Method: SAXS/SANS SASDDU6: The ferredoxin protease, FusC, E83A mutant (Ferredoxin protease E83A mutant, FusC E83A) Method: SAXS/SANS SASDDV6: The ferredoxin protease, FusC, E83A mutant + 3 µM Arabidopsis ferredoxin Method: SAXS/SANS SASDDW6: The ferredoxin protease, FusC, E83A mutant + 5 µM Arabidopsis ferredoxin Method: SAXS/SANS SASDDX6: The ferredoxin protease, FusC, E83A mutant + 10 µM Arabidopsis ferredoxin Method: SAXS/SANS SASDDY6: The ferredoxin protease, FusC, E83A mutant + 20 µM Arabidopsis ferredoxin Method: SAXS/SANS SASDDZ6: The ferredoxin protease, FusC, E83A mutant + 30 µM Arabidopsis ferredoxin Method: SAXS/SANS PDB-6b03: The crystal structure of the ferredoxin protease FusC in complex with its substrate plant ferredoxin Method: X-RAY DIFFRACTION / Resolution: 2.7 Å PDB-6b05: The Crystal Structure of the Ferredoxin Protease FusC E83A mutant in complex with Arabidopsis Ferredoxin Method: X-RAY DIFFRACTION / Resolution: 1.9 Å PDB-6brs: The Crystal Structure of the Ferredoxin Protease FusC in complex with Arabidopsis Ferredoxin, Ethylmercury phosphate soaked dataset Method: X-RAY DIFFRACTION / Resolution: 2.3 Å
Chemicals	ChemComp-HOH: WATER ChemComp-ZN: Unknown entry ChemComp-PO4: PHOSPHATE ION ChemComp-HG: Unknown entry
Source	pectobacterium atrosepticum scri1043 (bacteria) arabidopsis thaliana (thale cress) pectobacterium atrosepticum (strain scri 1043 / atcc baa-672) (bacteria)
Keywords	HYDROLASE / M16 Protease / Ferredoxin cleavage / Iron Acquisition / Ferredoxin Binding