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Structural and biochemical studies identify tobacco SABP2 as a methyl salicylate esterase and implicate it in plant innate immunity

Forouhar, F ; Yang, Y ; Kumar, D ; Chen, Y ; Fridman, E ; Park, S.W ; Chiang, Y ; Acton, T.B ; Montelione, G.T ; Pichersky, E

Journal of the American Chemical Society, 2005-02, Vol.102 (5), p.1773-1778 [Peer Reviewed Journal]

United States: National Academy of Sciences

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Title:
Structural and biochemical studies identify tobacco SABP2 as a methyl salicylate esterase and implicate it in plant innate immunity
Author: Forouhar, F ; Yang, Y ; Kumar, D ; Chen, Y ; Fridman, E ; Park, S.W ; Chiang, Y ; Acton, T.B ; Montelione, G.T ; Pichersky, E
Subjects: Active sites ; Amino Acid Sequence ; BASIC BIOLOGICAL SCIENCES ; BIOCHEMISTRY ; Biological Sciences ; Botany ; Carbonic Anhydrases - metabolism ; Catalase - metabolism ; Crystal structure ; Crystallography, X-Ray - methods ; Dimers ; enzyme activity ; Enzymes ; ESTERASES ; IMMUNITY ; Immunity, Innate ; Infections ; Mesas ; methyl salicylate ; methyl salicylate esterase ; Models, Molecular ; Molecular Sequence Data ; Monomers ; national synchrotron light source ; Nicotiana - enzymology ; Nicotiana tabacum ; plant proteins ; Plant Proteins - chemistry ; Plant Proteins - metabolism ; Plants ; protein structure ; Protein Structure, Secondary ; salicylic acid-binding protein 2 ; Sequence Alignment ; Sequence Homology, Amino Acid ; Signal transduction ; Solvents ; TOBACCO
Is Part Of: Journal of the American Chemical Society, 2005-02, Vol.102 (5), p.1773-1778
Notes: http://dx.doi.org/10.1073/pnas.0409227102
ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-1
content type line 23
DOE/OFFICE OF SCIENCE
DE-AC02-98CH10886
BNL-76581-2005-JA
Communicated by Anthony R. Cashmore, University of Pennsylvania, Philadelphia, PA, December 10, 2004
To whom correspondence may be addressed. E-mail: lelx@umich.edu, dfk8@cornell.edu, or tong@como.bio.columbia.edu.
Abbreviations: SAR, systemic acquired resistance; SA, salicylic acid; MeSA, methyl salicylate; SABP, SA-binding protein; HNL, hydroxynitrile lyase; pNP, para-nitrophenyl; MeJA, methyl jasmonate; MeIAA, methylindoleacetic acid.
Y.Y. and D.K. contributed equally to this work.
Data deposition: The atomic coordinates have been deposited in the Protein Data Bank, www.pdb.org (PDB ID codes 1Y7H, 1Y7I, and IXKL).
Description: Salicylic acid (SA) is a critical signal for the activation of plant defense responses against pathogen infections. We recently identified SA-binding protein 2 (SABP2) from tobacco as a protein that displays high affinity for SA and plays a crucial role in the activation of systemic acquired resistance to plant pathogens. Here we report the crystal structures of SABP2, alone and in complex with SA at up to 2.1-Å resolution. The structures confirm that SABP2 is a member of the α/β hydrolase superfamily of enzymes, with Ser-81, His-238, and Asp-210 as the catalytic triad. SA is bound in the active site and is completely shielded from the solvent, consistent with the high affinity of this compound for SABP2. Our biochemical studies reveal that SABP2 has strong esterase activity with methyl salicylate as the substrate, and that SA is a potent product inhibitor of this catalysis. Modeling of SABP2 with MeSA in the active site is consistent with all these biochemical observations. Our results suggest that SABP2 may be required to convert MeSA to SA as part of the signal transduction pathways that activate systemic acquired resistance and perhaps local defense responses as well.
Publisher: United States: National Academy of Sciences
Language: English

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Structural and biochemical studies identify tobacco SABP2 as a methyl salicylate esterase and implicate it in plant innate immunity

Forouhar, F ; Yang, Y ; Kumar, D ; Chen, Y ; Fridman, E ; Park, S.W ; Chiang, Y ; Acton, T.B ; Montelione, G.T ; Pichersky, E

United States: National Academy of Sciences

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