Unusual N-terminal ααβαββα Fold of PilQ fromThermus thermophilusMediates Ring Formation and Is Essential for Piliation
Published 2012 View Full Article
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Title
Unusual N-terminal ααβαββα Fold of PilQ fromThermus thermophilusMediates Ring Formation and Is Essential for Piliation
Authors
Keywords
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Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 287, Issue 11, Pages 8484-8494
Publisher
American Society for Biochemistry & Molecular Biology (ASBMB)
Online
2012-01-18
DOI
10.1074/jbc.m111.334912
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Note: Only part of the references are listed.- Identification and characterization of a unique, zinc-containing transport ATPase essential for natural transformation in Thermus thermophilus HB27
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- A conserved structural motif mediates formation of the periplasmic rings in the type III secretion system
- (2009) Thomas Spreter et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Structure, function and regulation of the conserved serine proteases DegP and DegS of Escherichia coli
- (2009) Michael Meltzer et al. RESEARCH IN MICROBIOLOGY
- Crystal Structure of the N-Terminal Domain of the Secretin GspD from ETEC Determined with the Assistance of a Nanobody
- (2009) Konstantin V. Korotkov et al. STRUCTURE
- The role of single subunits of the DNA transport machinery ofThermus thermophilusHB27 in DNA binding and transport
- (2008) Cornelia Schwarzenlander et al. ENVIRONMENTAL MICROBIOLOGY
- Omp85Tt from Thermus thermophilus HB27: an Ancestral Type of the Omp85 Protein Family
- (2008) J. Nesper et al. JOURNAL OF BACTERIOLOGY
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