X-ray crystal structures of the type IVb secretion system DotB ATPases

Protein Science : a Publication of the Protein Society
Marie S Prevost, Gabriel Waksman

Abstract

Human infections by the intracellular bacterial pathogen Legionella pneumophila result in a severe form of pneumonia, the Legionnaire's disease. L. pneumophila utilizes a Type IVb secretion (T4bS) system termed "dot/icm" to secrete protein effectors to the host cytoplasm. The dot/icm system is powered at least in part by a functionally critical AAA+ ATPase, a protein called DotB, thought to belong to the VirB11 family of proteins. Here we present the crystal structure of DotB at 3.19 Å resolution, in its hexameric form. We observe that DotB is in fact a structural intermediate between VirB11 and PilT family proteins, with a PAS-like N-terminal domain coupled to a RecA-like C-terminal domain. It also shares critical structural elements only found in PilT. The structure also reveals two conformers, termed α and β, with an αβαβαβ configuration. The existence of α and β conformers in this class of proteins was confirmed by solving the structure of DotB from another bacterial pathogen, Yersinia, where, intriguingly, we observed an ααβααβ configuration. The two conformers co-exist regardless of the nucleotide-bound states of the proteins. Our investigation therefore reveals that these ATPases can adopt a wider range of conformational...Continue Reading

References

Mar 21, 1998·Proceedings of the National Academy of Sciences of the United States of America·G SegalH A Shuman
May 3, 2003·The EMBO Journal·Savvas N SavvidesGabriel Waksman
Jul 21, 2004·Journal of Computational Chemistry·Eric F PettersenThomas E Ferrin
May 1, 1997·Acta Crystallographica. Section D, Biological Crystallography·G N MurshudovE J Dodson
Dec 2, 2004·Acta Crystallographica. Section D, Biological Crystallography·E Krissinel, K Henrick
Jan 5, 2005·Journal of Bacteriology·Kelly G AukemaKatrina T Forest
May 30, 2006·Journal of Molecular Biology·Stephen HareGabriel Waksman
Aug 1, 2007·Journal of Applied Crystallography·Airlie J McCoyRandy J Read
Feb 4, 2010·Acta Crystallographica. Section D, Biological Crystallography·Wolfgang Kabsch
Feb 4, 2010·Acta Crystallographica. Section D, Biological Crystallography·Paul D AdamsPeter H Zwart
Apr 13, 2010·Acta Crystallographica. Section D, Biological Crystallography·P EmsleyK Cowtan
May 12, 2010·Nucleic Acids Research·Liisa Holm, Päivi Rosenström
Apr 5, 2011·Acta Crystallographica. Section D, Biological Crystallography·Martyn D WinnKeith S Wilson
Oct 13, 2011·Molecular Systems Biology·Fabian SieversDesmond G Higgins
Apr 23, 2014·Nucleic Acids Research·Xavier Robert, Patrice Gouet
Dec 3, 2014·Bioorganic & Medicinal Chemistry·James R SayerAlethea B Tabor
Jan 16, 2015·Chemical Biology & Drug Design·Ségolène RuerHan Remaut
Feb 27, 2016·Molecular Microbiology·Jorge Ripoll-RozadaIgnacio Arechaga
May 6, 2017·Nature Communications·Matthew McCallumP Lynne Howell

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Datasets Mentioned

BETA
321630

Methods Mentioned

BETA
X‐ray
gel filtration
PCR

Software Mentioned

CCP4 suite
XDS
Chimera
COOT
PHASER
PilT
PyMol
PyMOL Molecular Graphics System
CHAINSAW
PDBePISA Server

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