- EMDB-27797: Cryo-EM structure of bundle-forming pilus extension ATPase from E... -
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Basic information
Entry
Database: EMDB / ID: EMD-27797
Title
Cryo-EM structure of bundle-forming pilus extension ATPase from E.coli in the presence of ADP
Map data
Sample
Organelle or cellular component: Bundle-forming pilus extension ATPase from enteropathogenic E. coli in the presence of ADP
Protein or peptide: BfpD
Ligand: MAGNESIUM ION
Ligand: ADENOSINE-5'-DIPHOSPHATE
Ligand: ZINC ION
Keywords
BfpD / AAA-ATPase / Structural protein / Type 4 pilus accessory protein
Function / homology
Type II/IV secretion system protein / Type II/IV secretion system protein / ATP hydrolysis activity / P-loop containing nucleoside triphosphate hydrolase / ATP binding / plasma membrane / BfpD
Function and homology information
Biological species
Escherichia coli (E. coli)
Method
single particle reconstruction / cryo EM / Resolution: 3.1 Å
National Institutes of Health/National Institute of Arthritis and Musculoskeletal and Skin Diseases (NIH/NIAMS)
R01 AR068431
United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
U24 GM116790
United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
R56A/111767
United States
Citation
Journal: mBio / Year: 2022 Title: Cryo-EM Structure of the Type IV Pilus Extension ATPase from Enteropathogenic Escherichia coli. Authors: Ashok R Nayak / Pradip K Singh / Jinlei Zhao / Montserrat Samsó / Michael S Donnenberg / Abstract: Type 4 pili (T4P) are retractable surface appendages found on numerous bacteria and archaea that play essential roles in various microbial functions, including host colonization by pathogens. An ...Type 4 pili (T4P) are retractable surface appendages found on numerous bacteria and archaea that play essential roles in various microbial functions, including host colonization by pathogens. An ATPase is required for T4P extension, but the mechanism by which chemical energy is transduced to mechanical energy for pilus extension has not been elucidated. Here, we report the cryo-electron microscopy (cryo-EM) structure of the BfpD ATPase from enteropathogenic Escherichia coli (EPEC) in the presence of either ADP or a mixture of ADP and AMP-PNP. Both structures, solved at 3 Å resolution, reveal the typical toroid shape of AAA+ ATPases and unambiguous 6-fold symmetry. This 6-fold symmetry contrasts with the 2-fold symmetry previously reported for other T4P extension ATPase structures, all of which were from thermophiles and solved by crystallography. In the presence of the nucleotide mixture, BfpD bound exclusively AMP-PNP, and this binding resulted in a modest outward expansion in comparison to the structure in the presence of ADP, suggesting a concerted model for hydrolysis. molecular models reveal a partially open configuration of all subunits where the nucleotide binding site may not be optimally positioned for catalysis. ATPase functional studies reveal modest activity similar to that of other extension ATPases, while calculations indicate that this activity is insufficient to power pilus extension. Our results reveal that, despite similarities in primary sequence and tertiary structure, T4P extension ATPases exhibit divergent quaternary configurations. Our data raise new possibilities regarding the mechanism by which T4P extension ATPases power pilus formation. Type 4 pili are hairlike surface appendages on many bacteria and archaea that can be extended and retracted with tremendous force. They play a critical role in disease caused by several deadly human pathogens. Pilus extension is made possible by an enzyme that converts chemical energy to mechanical energy. Here, we describe the three-dimensional structure of such an enzyme from a human pathogen in unprecedented detail, which reveals a mechanism of action that has not been seen previously among enzymes that power type 4 pilus extension.
Entire : Bundle-forming pilus extension ATPase from enteropathogenic E. co...
Entire
Name: Bundle-forming pilus extension ATPase from enteropathogenic E. coli in the presence of ADP
Components
Organelle or cellular component: Bundle-forming pilus extension ATPase from enteropathogenic E. coli in the presence of ADP
Protein or peptide: BfpD
Ligand: MAGNESIUM ION
Ligand: ADENOSINE-5'-DIPHOSPHATE
Ligand: ZINC ION
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Supramolecule #1: Bundle-forming pilus extension ATPase from enteropathogenic E. co...
Supramolecule
Name: Bundle-forming pilus extension ATPase from enteropathogenic E. coli in the presence of ADP type: organelle_or_cellular_component / ID: 1 / Parent: 0 / Macromolecule list: #1 / Details: BfpD ATPase with 5 mM MgCl2 and 1 mM ADP
Source (natural)
Organism: Escherichia coli (E. coli)
Molecular weight
Theoretical: 362 KDa
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Macromolecule #1: BfpD
Macromolecule
Name: BfpD / type: protein_or_peptide / ID: 1 / Number of copies: 6 / Enantiomer: LEVO
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