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Structural insights into the mechanism of Type IVa pilus extension and retraction ATPase motors.

DIR@IMTECH: CSIR-Institute of Microbial Technology

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Title Structural insights into the mechanism of Type IVa pilus extension and retraction ATPase motors.
 
Creator Solanki, Vipul
Kapoor, Srajan
Thakur, Krishan Gopal
 
Subject QR Microbiology
 
Description 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.
 
Publisher Wiley
 
Date 2018-08-01
 
Type Article
PeerReviewed
 
Relation https://doi.org/10.1111/febs.14619
http://crdd.osdd.net/open/2159/
 
Identifier Solanki, Vipul and Kapoor, Srajan and Thakur, Krishan Gopal (2018) Structural insights into the mechanism of Type IVa pilus extension and retraction ATPase motors. The FEBS journal, 285 (18). pp. 3402-3421. ISSN 1742-4658