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Structure paper

TitleProtease-associated import systems are widespread in Gram-negative bacteria.
Journal, issue, pagesPLoS Genet, Vol. 15, Issue 10, Page e1008435, Year 2019
Publish dateOct 15, 2019
AuthorsRhys Grinter / Pok Man Leung / Lakshmi C Wijeyewickrema / Dene Littler / Simone Beckham / Robert N Pike / Daniel Walker / Chris Greening / Trevor Lithgow /
PubMed AbstractBacteria have evolved sophisticated uptake machineries in order to obtain the nutrients required for growth. Gram-negative plant pathogens of the genus Pectobacterium obtain iron from the protein ...Bacteria have evolved sophisticated uptake machineries in order to obtain the nutrients required for growth. Gram-negative plant pathogens of the genus Pectobacterium obtain iron from the protein ferredoxin, which is produced by their plant hosts. This iron-piracy is mediated by the ferredoxin uptake system (Fus), a gene cluster encoding proteins that transport ferredoxin into the bacterial cell and process it proteolytically. In this work we show that gene clusters related to the Fus are widespread in bacterial species. Through structural and biochemical characterisation of the distantly related Fus homologues YddB and PqqL from Escherichia coli, we show that these proteins are analogous to components of the Fus from Pectobacterium. The membrane protein YddB shares common structural features with the outer membrane ferredoxin transporter FusA, including a large extracellular substrate binding site. PqqL is an active protease with an analogous periplasmic localisation and iron-dependent expression to the ferredoxin processing protease FusC. Structural analysis demonstrates that PqqL and FusC share specific features that distinguish them from other members of the M16 protease family. Taken together, these data provide evidence that protease associated import systems analogous to the Fus are widespread in Gram-negative bacteria.
External linksPLoS Genet / PubMed:31613892 / PubMed Central
MethodsSAS (X-ray synchrotron) / X-ray diffraction
Resolution2 - 2.6 Å
Structure data

SASDFB6:
The periplasmically localised protease PqqL from Escherichia coli
Method: SAXS/SANS

PDB-6ofr:
The crystal structure of the outer membrane transporter YddB from Escherichia coli
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-6ofs:
The crystal structure of the periplasmic protease PqqL from Escherichia coli
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

PDB-6oft:
The crystal structure of the first half of the periplasmic protease PqqL from Escherichia coli
Method: X-RAY DIFFRACTION / Resolution: 2.0 Å

Chemicals

ChemComp-BOG:
octyl beta-D-glucopyranoside / detergent*YM

ChemComp-MG:
Unknown entry

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-ZN:
Unknown entry

ChemComp-CL:
Unknown entry

ChemComp-PO4:
PHOSPHATE ION

Source
  • escherichia coli (strain k12) (bacteria)
  • escherichia coli (E. coli)
KeywordsTRANSPORT PROTEIN / Protein Transport / Gram-negative bacteria / Outer membrane / Nutrient Uptake / TonB-Dependent Transporter / HYDROLASE / Protease / M16 Family / Processing Protease

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