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Title: Crystal Structure of a Type IV Pilus Assembly ATPase: Insights into the Molecular Mechanism of PilB from Thermus thermophilus

Type IV pili (T4P) mediate bacterial motility and virulence. The PilB/GspE family ATPases power the assembly of T4P and type 2 secretion systems. We determined the structure of the ATPase region of PilB (PilB ATP) in complex with ATPγS to provide a model of a T4P assembly ATPase and a view of a PilB/GspE family hexamer at better than 3-Å resolution. Spatial positioning and conformations of the protomers suggest a mechanism of force generation. All six PilB ATP protomers contain bound ATPγS. Two protomers form a closed conformation poised for ATP hydrolysis. The other four molecules assume an open conformation but separate into two pairs with distinct active-site accessibilities. We propose that one pair represents the post-hydrolysis phase while the other pair appears poised for ADP/ATP exchange. In conclusion, collectively, the data suggest that T4P assembly is powered by coordinating concurrent substrate binding with ATP hydrolysis across the PilB hexamer.
Authors:
 [1] ;  [1] ;  [2] ;  [1] ;  [1]
  1. Virginia Polytechnic Inst. and State Univ. (Virginia Tech), Blacksburg, VA (United States). Dept. of Biological Sciences
  2. Brookhaven National Lab. (BNL), Upton, NY (United States). Biology Dept.
Publication Date:
Report Number(s):
BNL-113445-2017-JA
Journal ID: ISSN 0969-2126
Grant/Contract Number:
SC00112704; MCB-1417726
Type:
Published Article
Journal Name:
Structure
Additional Journal Information:
Journal Volume: 24; Journal Issue: 11; Journal ID: ISSN 0969-2126
Publisher:
Elsevier
Research Org:
Brookhaven National Laboratory (BNL), Upton, NY (United States)
Sponsoring Org:
USDOE Office of Science (SC), Biological and Environmental Research (BER) (SC-23); National Science Foundation (NSF); National Institutes of Health (NIH)
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES
OSTI Identifier:
1406641
Alternate Identifier(s):
OSTI ID: 1341698; OSTI ID: 1398550