Adenylylation control by intra-or intermolecular active-site obstruction in Fic proteins

Nature

Volumn 482, Issue 7383, 2012, Pages 107-110

  Engel, Philipp ^a,b   Goepfert, Arnaud ^a   Stanger, Frédéric V ^a   Harms, Alexander ^a   Schmidt, Alexander ^a   Schirmer, Tilman ^a   Dehio, Christoph ^a  

^a UNIVERSITY OF BASEL   (Switzerland)

^b YALE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; ANTITOXIN; BACTERIAL PROTEIN; BACTERIAL TOXIN; GLUTAMIC ACID; MUTANT PROTEIN; PROTEIN FILAMENTATION INDUCED BY CYCLIC AMP; UNCLASSIFIED DRUG;

AMINO ACID; BACTERIUM; CATALYSIS; CELL ORGANELLE; ENVIRONMENTAL FACTOR; ENZYME ACTIVITY; HOMOLOGY; INHIBITION; INHIBITOR; MOLECULAR ANALYSIS; PATHOGENICITY; PROTEIN; SIGNALING; TOXIN;

ADENYLATION; ALPHA HELIX; AMINO TERMINAL SEQUENCE; ARTICLE; BACTERIAL GROWTH; BARTONELLA; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; MOLECULAR MODEL; NEISSERIA MENINGITIDIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN MOTIF; SHEWANELLA ONEIDENSIS; STRUCTURAL HOMOLOGY;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BARTONELLA; CARRIER PROTEINS; CATALYSIS; CATALYTIC DOMAIN; CYCLIC AMP; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; GLUTAMIC ACID; HUMANS; MEMBRANE PROTEINS; MICROBIAL VIABILITY; MODELS, MOLECULAR; MOLECULAR WEIGHT; NEISSERIA MENINGITIDIS; PROTEIN STRUCTURE, TERTIARY; SHEWANELLA;

BACTERIA (MICROORGANISMS); BARTONELLA SCHOENBUCHENSIS; MAMMALIA; NEISSERIA MENINGITIDIS; SHEWANELLA ONEIDENSIS;

EID: 84856417389     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature10729     Document Type: Article

References (32)

1. Worby, C. A. et al. The fic domain: regulation of cell signaling by adenylylation. Mol. Cell 34, 93-103 (2009).
2. Yarbrough, M. L. et al. AMPylation of Rho GTPases by Vibrio VopS disrupts effector binding and downstream signaling. Science 323, 269-272 (2009).
3. Roy, C. R. & Mukherjee, S. Bacterial FIC proteins AMP up infection. Sci. Signal. 2, pe14 (2009).
4. Mattoo, S. et al. Comparative analysis of Histophilus somni immunoglobulinbinding protein A (IbpA) with other Fic domain-containing enzymes reveals differences in substrate and nucleotide specificities. J. Biol. Chem. 286, 32834-32842 (2011).
5. Luong, P. et al. Kinetic andstructural insights into themechanismofAMPylation by VopS Fic domain. J. Biol. Chem. 285, 20155-20163 (2010).
6. Xiao, J., Worby, C. A., Mattoo, S., Sankaran, B. & Dixon, J. E. Structural basis of Ficmediated adenylylation. Nature Struct. Mol. Biol. 17, 1004-1010 (2010).
7. Dehio, C. et al. Bartonella schoenbuchii sp. nov., isolated from the blood of wild roe deer. Int. J. Syst. Evol. Microbiol. 51, 1557-1565 (2001). (Pubitemid 32700653)
8. Engel, P. et al. Parallel evolution of a type IV secretion systemin radiating lineages of the host-restricted bacterial pathogen Bartonella. PLoS Genet. 7, e1001296 (2011).
9. Schulein, R. et al. A bipartite signal mediates the transfer of type IV secretion substrates of Bartonella henselae into human cells. Proc. Natl Acad. Sci. USA 102, 856-861 (2005). (Pubitemid 40282755)
10. Palanivelu, D. V. et al. Fic domain-catalyzed adenylylation: insight provided by the structural analysis of the type IV secretion system effector BepA. Protein Sci. 20, 492-499 (2011).
11. Utsumi, R., Nakamoto, Y., Kawamukai, M., Himeno, M. & Komano, T. Involvement of cyclic AMP and its receptor protein in filamentation of an Escherichia coli fic mutant. J. Bacteriol. 151, 807-812 (1982). (Pubitemid 13230477)
12. Engelberg-Kulka, H., Amitai, S., Kolodkin-Gal, I. & Hazan, R. Bacterial programmed cell death and multicellular behavior in bacteria. PLoS Genet. 2, e135 (2006).
13. Garcia-Pino, A. et al. Doc of prophage P1 is inhibited by its antitoxin partner Phd through fold complementation. J. Biol. Chem. 283, 30821-30827 (2008).
14. Kinch, L. N., Yarbrough, M. L., Orth, K. & Grishin, N. V. Fido, a novel AMPylation domain common to Fic, Doc, and AvrB. PLoS ONE 4, e5818 (2009).
15. Das, D. et al. Crystal structure of the Fic (Filamentation induced by cAMP) family protein SO4266 (gij24375750) from Shewanella oneidensis MR-1 at 1. 6A resolution. Proteins 75, 264-271 (2009).
16. Mukherjee, S. et al. Modulation of Rab GTPase function by a protein phosphocholine transferase. Nature 477, 103-106 (2011).
17. Söing, J., Biegert, A. & Lupas, A. N. The HHpred interactive server for protein homology detection and structure prediction. Nucleic Acids Res. 33, W244-W248 (2005). (Pubitemid 44529917)
18. Self, A. J. & Hall, A. Purification of recombinant Rho/Rac/G25K from Escherichia coli. Methods Enzymol. 256, 3-10 (1995).
19. Smith, S. J. & Rittinger, K. Preparation of GTPases for structural and biophysical analysis. Methods Mol. Biol. 189, 13-24 (2002).
20. Leslie, A. G. The integration of macromolecular diffraction data. Acta Crystallogr. D 62, 48-57 (2006).
21. Collaborative Computational Project, Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50, 760-763 (1994).
22. McCoy, A. J. et al. Phaser crystallographic software. J. Appl. Crystallogr. 40, 658-674 (2007). (Pubitemid 47080256)
23. Murshudov, G. N., Vagin, A. A. & Dodson, E. J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D 53, 240-255 (1997). (Pubitemid 27235885)
24. Adams, P. D. et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D 66, 213-221 (2010).
25. Emsley, P. & Cowtan, K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D 60, 2126-2132 (2004). (Pubitemid 41742764)
26. Jones, D. T. Protein secondary structure prediction based on position-specific scoring matrices. J. Mol. Biol. 292, 195-202 (1999). (Pubitemid 29435759)
27. Price, M. N., Dehal, P. S. & Arkin, A. P. FastTree 2-approximately maximumlikelihood trees for large alignments. PLoS ONE 5, e9490 (2010).
28. Stamatakis, A. RAxML-VI-HPC: maximumlikelihood-based phylogenetic analyses with thousands of taxa and mixed models. Bioinformatics 22, 2688-2690 (2006). (Pubitemid 44642609)
29. Schmidt, A. et al. Absolute quantification of microbial proteomes at different states by directed mass spectrometry. Mol. Syst. Biol. 7, 510 (2011).
30. Zheng, L., Baumann, U. & Reymond, J. L. An efficient one-step site-directed and site-saturation mutagenesis protocol. Nucleic Acids Res. 32, e115 (2004).
31. Dehio, C. & Meyer, M. Maintenance of broad-host-range incompatibility group P and group Q plasmids and transposition of Tn5 in Bartonella henselae following conjugal plasmid transfer from Escherichia coli. J. Bacteriol. 179, 538-540 (1997). (Pubitemid 27030408)
32. Rhomberg, T. A., Truttmann, M. C., Guye, P., Ellner, Y. & Dehio, C. A translocated protein of Bartonella henselae interferes with endocytic uptake of individual bacteria and triggers uptake of large bacterial aggregates via the invasome. Cell. Microbiol. 11, 927-945 (2009).