2EWW

Crystal Structure of the Pilus Retraction Motor PilT and Bound ATP

Summary for 2EWW

• Entry DOI: 10.2210/pdb2eww/pdb
• Descriptor: twitching motility protein PilT, ADENOSINE-5'-TRIPHOSPHATE (3 entities in total)
• Functional Keywords: pilus retraction motor, atpase, hexameric pilt, protein transport
• Biological source: Aquifex aeolicus
• Total number of polymer chains: 1
• Total formula weight: 43066.58

Authors

Satyshur, K.A.,Forest, K.T. (deposition date: 2005-11-07, release date: 2006-11-21, Last modification date: 2024-10-30)

Primary citation

Satyshur, K.A.,Worzalla, G.A.,Meyer, L.S.,Heiniger, E.K.,Aukema, K.G.,Misic, A.M.,Forest, K.T.
Crystal structures of the pilus retraction motor PilT suggest large domain movements and subunit cooperation drive motility.
Structure, 15:363-376, 2007

PubMed Abstract: PilT is a hexameric ATPase required for bacterial type IV pilus retraction and surface motility. Crystal structures of ADP- and ATP-bound Aquifex aeolicus PilT at 2.8 and 3.2 A resolution show N-terminal PAS-like and C-terminal RecA-like ATPase domains followed by a set of short C-terminal helices. The hexamer is formed by extensive polar subunit interactions between the ATPase core of one monomer and the N-terminal domain of the next. An additional structure captures a nonsymmetric PilT hexamer in which approach of invariant arginines from two subunits to the bound nucleotide forms an enzymatically competent active site. A panel of pilT mutations highlights the importance of the arginines, the PAS-like domain, the polar subunit interface, and the C-terminal helices for retraction. We present a model for ATP binding leading to dramatic PilT domain motions, engagement of the arginine wire, and subunit communication in this hexameric motor. Our conclusions apply to the entire type II/IV secretion ATPase family.

PubMed: 17355871
DOI: 10.1016/j.str.2007.01.018

Experimental method

X-RAY DIFFRACTION (3.2 Å)