5ZFR

Crystal structure of PilB, an extension ATPase motor of Type IV pilus, from Geobacter sulfurreducens

Summary for 5ZFR

• Entry DOI: 10.2210/pdb5zfr/pdb
• Descriptor: Type IV pilus biogenesis ATPase PilB, ZINC ION, PHOSPHATE ION, ... (4 entities in total)
• Functional Keywords: extension motor, transport protein
• Biological source: Geobacter sulfurreducens PCA
• Total number of polymer chains: 3
• Total formula weight: 193518.31

Authors

Thakur, K.G.,Solanki, V.,Kapoor, S. (deposition date: 2018-03-06, release date: 2018-09-19, Last modification date: 2023-11-22)

Primary citation

Solanki, V.,Kapoor, S.,Thakur, K.G.
Structural insights into the mechanism of Type IVa pilus extension and retraction ATPase motors
FEBS J., 285:3402-3421, 2018

PubMed Abstract: Type IVa pili are bacterial appendages involved in diverse physiological processes, including electron transfer in Geobacter sulfurreducens. ATP hydrolysis coupled with conformational changes powers the extension (PilB) and retraction (PilT) motors in the pilus machinery. We report the unliganded crystal structures of the core ATPase domain of PilB and PilT-4 from G. sulfurreducens at 3.1 and 2.6 Å resolution, respectively. PilB structure revealed three distinct conformations, that is, open, closed, and open' which were previously proposed to be mediated by ATP/ADP binding. PilT-4 subunits, on the other hand, were observed in the closed state conformation. We further report that both PilB and PilT-4 hexamers have two high-affinity ATP-binding sites. Comparative structural analysis and solution data presented here supports the "symmetric rotary model" for these ATPase motors. Our data further suggest that pores of these motors rotate either clockwise or counterclockwise to facilitate assembly or disassembly of right-handed or left-handed pilus.

PubMed: 30066435
DOI: 10.1111/febs.14619

Experimental method

X-RAY DIFFRACTION (3.1 Å)