Crystal structure of the type III effector AvrB from Pseudomonas syringae

被引:40
作者
Lee, CC
Wood, MD
Ng, K
Andersen, CB
Liu, Y
Luginbühl, P
Spraggon, G
Katagiri, F
机构
[1] Novartis Res Fdn, Genom Inst, San Diego, CA 92121 USA
[2] Torrey Mesa Res Inst, San Diego, CA 92121 USA
[3] Syngenta Res & Technol, San Diego, CA 92121 USA
[4] Univ Maryland, Dept Sci Biol, Baltimore, MD 21250 USA
关键词
D O I
10.1016/j.str.2004.02.013
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
AvrB is a Pseudomonas syringae type III effector protein that is translocated into host plant cells during attempted pathogenesis. Arabidopsis harboring the corresponding resistance protein RPM1 can detect AvrB and mount a rapid host defense response, thus avoiding active infection. In the plant cell, AvrB induces phosphorylation of RIN4, a key component in AvrB/RPM1 recognition. Although the AvrB/RPM1 system is among the best characterized of the numerous bacterial effector/plant resistance protein systems involved in plant disease resistance and pathogenesis, the details of the molecular recognition mechanism are still unclear. To gain further insights, the crystal structure of AvrB was determined. The 2.2 Angstrom structure exhibits a novel mixed alpha/beta bilobal fold. Aided by the structural information, we demonstrate that one lobe is the determinant of AvrB/RPM1 recognition specificity. This structural information and preliminary structure-function studies provide a framework for the future understanding of AvrB function on the molecular level.
引用
收藏
页码:487 / 494
页数:8
相关论文
共 31 条
[1]   The Pseudomonas syringae Hrp pathogenicity island has a tripartite mosaic structure composed of a cluster of type III secretion genes bounded by exchangeable effector and conserved effector loci that contribute to parasitic fitness and pathogenicity in plants [J].
Alfano, JR ;
Charkowski, AO ;
Deng, WL ;
Badel, JL ;
Petnicki-Ocwieja, T ;
van Dijk, K ;
Collmer, A .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2000, 97 (09) :4856-4861
[2]   Gapped BLAST and PSI-BLAST: a new generation of protein database search programs [J].
Altschul, SF ;
Madden, TL ;
Schaffer, AA ;
Zhang, JH ;
Zhang, Z ;
Miller, W ;
Lipman, DJ .
NUCLEIC ACIDS RESEARCH, 1997, 25 (17) :3389-3402
[3]   Initiation of RPS2-specified disease resistance in Arabidopsis is coupled to the AvrRpt2-directed elimination of RIN4 [J].
Axtell, MJ ;
Staskawicz, BJ .
CELL, 2003, 112 (03) :369-377
[4]   Plant disease resistance triggered by pathogen-derived molecules: refined models of specific recognition [J].
Bonas, U ;
Lahaye, T .
CURRENT OPINION IN MICROBIOLOGY, 2002, 5 (01) :44-50
[5]   The Arabidopsis thaliana RPM1 disease resistance gene product is a peripheral plasma membrane protein that is degraded coincident with the hypersensitive response [J].
Boyes, DC ;
Nam, J ;
Dangl, JL .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1998, 95 (26) :15849-15854
[6]  
Brunger AT, 1998, ACTA CRYSTALLOGR D, V54, P905, DOI 10.1107/s0907444998003254
[7]   Comparison of the genomes of two Xanthomonas pathogens with differing host specificities [J].
A. C. R. da Silva ;
J. A. Ferro ;
F. C. Reinach ;
C. S. Farah ;
L. R. Furlan ;
R. B. Quaggio ;
C. B. Monteiro-Vitorello ;
M. A. Van Sluys ;
N. F. Almeida ;
L. M. C. Alves ;
A. M. do Amaral ;
M. C. Bertolini ;
L. E. A. Camargo ;
G. Camarotte ;
F. Cannavan ;
J. Cardozo ;
F. Chambergo ;
L. P. Ciapina ;
R. M. B. Cicarelli ;
L. L. Coutinho ;
J. R. Cursino-Santos ;
H. El-Dorry ;
J. B. Faria ;
A. J. S. Ferreira ;
R. C. C. Ferreira ;
M. I. T. Ferro ;
E. F. Formighieri ;
M. C. Franco ;
C. C. Greggio ;
A. Gruber ;
A. M. Katsuyama ;
L. T. Kishi ;
R. P. Leite ;
E. G. M. Lemos ;
M. V. F. Lemos ;
E. C. Locali ;
M. A. Machado ;
A. M. B. N. Madeira ;
N. M. Martinez-Rossi ;
E. C. Martins ;
J. Meidanis ;
C. F. M. Menck ;
C. Y. Miyaki ;
D. H. Moon ;
L. M. Moreira ;
M. T. M. Novo ;
V. K. Okura ;
M. C. Oliveira ;
V. R. Oliveira ;
H. A. Pereira .
Nature, 2002, 417 (6887) :459-463
[8]   Plant pathogens and integrated defence responses to infection [J].
Dangl, JL ;
Jones, JDG .
NATURE, 2001, 411 (6839) :826-833
[9]   Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods [J].
delaFortelle, E ;
Bricogne, G .
MACROMOLECULAR CRYSTALLOGRAPHY, PT A, 1997, 276 :472-494
[10]   Type III secretion machines:: Bacterial devices for protein delivery into host cells [J].
Galán, JE ;
Collmer, A .
SCIENCE, 1999, 284 (5418) :1322-1328