5TSH

PilB from Geobacter metallireducens bound to AMP-PNP

Summary for 5TSH

• Entry DOI: 10.2210/pdb5tsh/pdb
• Related: 5TSG
• Descriptor: Type IV pilus biogenesis ATPase PilB, ZINC ION, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (6 entities in total)
• Functional Keywords: pilb, pilus, type iva pilus, extension, atp-binding protein
• Biological source: Geobacter metallireducens (strain GS-15 / ATCC 53774 / DSM 7210)
• Total number of polymer chains: 6
• Total formula weight: 392631.75

Authors

McCallum, M.,Tammam, S.,Khan, A.,Burrows, L.,Howell, P.L. (deposition date: 2016-10-28, release date: 2017-05-17, Last modification date: 2023-10-04)

Primary citation

McCallum, M.,Tammam, S.,Khan, A.,Burrows, L.L.,Howell, P.L.
The molecular mechanism of the type IVa pilus motors.
Nat Commun, 8:15091-15091, 2017

PubMed Abstract: Type IVa pili are protein filaments essential for virulence in many bacterial pathogens; they extend and retract from the surface of bacterial cells to pull the bacteria forward. The motor ATPase PilB powers pilus assembly. Here we report the structures of the core ATPase domains of Geobacter metallireducens PilB bound to ADP and the non-hydrolysable ATP analogue, AMP-PNP, at 3.4 and 2.3 Å resolution, respectively. These structures reveal important differences in nucleotide binding between chains. Analysis of these differences reveals the sequential turnover of nucleotide, and the corresponding domain movements. Our data suggest a clockwise rotation of the central sub-pores of PilB, which through interactions with PilC, would support the assembly of a right-handed helical pilus. Our analysis also suggests a counterclockwise rotation of the C2 symmetric PilT that would enable right-handed pilus disassembly. The proposed model provides insight into how this family of ATPases can power pilus extension and retraction.

PubMed: 28474682
DOI: 10.1038/ncomms15091

Experimental method

X-RAY DIFFRACTION (2.3 Å)