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
Full text not available from this repository. (Request a copy)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.
| Item Type: | Article |
|---|---|
| Additional Information: | Copyright of this article belongs to John Wiley & Sons. |
| Uncontrolled Keywords: | Structural data are available in the RCSB PDB database under the PDB ID 5ZFQ (PilT-4), 5ZFR (PilB). |
| Subjects: | Q Science > QR Microbiology |
| Depositing User: | Dr. K.P.S.Sengar |
| Date Deposited: | 18 Mar 2019 16:56 |
| Last Modified: | 18 Mar 2019 16:56 |
| URI: | http://crdd.osdd.net/open/id/eprint/2159 |
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