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אסיף מאגר המחקר החקלאי
פותח על ידי קלירמאש פתרונות בע"מ -
Structural and biochemical studies identify tobacco SABP2 as a methyl salicylate esterase and implicate it in plant innate immunity
Year:
2005
Authors :
פרידמן, איל
;
.
Volume :
102
Co-Authors:
Forouhar, F., Department of Biological Sciences, NE Structural Genomics Consortium, Columbia University, New York, NY 10027, United States
Yang, Y., Dept. Molec., Cell., Devmtl. Biol., University of Michigan, Ann Arbor, MI 48109, United States
Kumar, D., Boyce Thompson Inst. for Plant Res., Tower Road, Ithaca, NY 14853, United States
Chen, Y., Department of Biological Sciences, NE Structural Genomics Consortium, Columbia University, New York, NY 10027, United States
Fridman, E., Dept. Molec., Cell., Devmtl. Biol., University of Michigan, Ann Arbor, MI 48109, United States
Park, S.W., Boyce Thompson Inst. for Plant Res., Tower Road, Ithaca, NY 14853, United States
Chiang, Y., Dept. of Molec. Biol. and Biochem., Rutgers University, Robert Wood Johnson Medical School, Piscataway, NJ 08854, United States, Department of Biochemistry, Robert Wood Johnson Medical School, Piscataway, NJ 08854, United States
Acton, T.B., Dept. of Molec. Biol. and Biochem., Rutgers University, Robert Wood Johnson Medical School, Piscataway, NJ 08854, United States, Department of Biochemistry, Robert Wood Johnson Medical School, Piscataway, NJ 08854, United States
Montelione, G.T., Dept. of Molec. Biol. and Biochem., Rutgers University, Robert Wood Johnson Medical School, Piscataway, NJ 08854, United States, Department of Biochemistry, Robert Wood Johnson Medical School, Piscataway, NJ 08854, United States
Pichersky, E., Dept. Molec., Cell., Devmtl. Biol., University of Michigan, Ann Arbor, MI 48109, United States
Klessig, D.F., Boyce Thompson Inst. for Plant Res., Tower Road, Ithaca, NY 14853, United States
Tong, L., Department of Biological Sciences, NE Structural Genomics Consortium, Columbia University, New York, NY 10027, United States
Facilitators :
From page:
1773
To page:
1778
(
Total pages:
6
)
Abstract:
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.
Note:
Related Files :
host pathogen interaction
hydrolase
Models, Molecular
unclassified drug
עוד תגיות
תוכן קשור
More details
DOI :
10.1073/pnas.0409227102
Article number:
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
22273
Last updated date:
02/03/2022 17:27
Creation date:
16/04/2018 23:50
You may also be interested in
Scientific Publication
Structural and biochemical studies identify tobacco SABP2 as a methyl salicylate esterase and implicate it in plant innate immunity
102
Forouhar, F., Department of Biological Sciences, NE Structural Genomics Consortium, Columbia University, New York, NY 10027, United States
Yang, Y., Dept. Molec., Cell., Devmtl. Biol., University of Michigan, Ann Arbor, MI 48109, United States
Kumar, D., Boyce Thompson Inst. for Plant Res., Tower Road, Ithaca, NY 14853, United States
Chen, Y., Department of Biological Sciences, NE Structural Genomics Consortium, Columbia University, New York, NY 10027, United States
Fridman, E., Dept. Molec., Cell., Devmtl. Biol., University of Michigan, Ann Arbor, MI 48109, United States
Park, S.W., Boyce Thompson Inst. for Plant Res., Tower Road, Ithaca, NY 14853, United States
Chiang, Y., Dept. of Molec. Biol. and Biochem., Rutgers University, Robert Wood Johnson Medical School, Piscataway, NJ 08854, United States, Department of Biochemistry, Robert Wood Johnson Medical School, Piscataway, NJ 08854, United States
Acton, T.B., Dept. of Molec. Biol. and Biochem., Rutgers University, Robert Wood Johnson Medical School, Piscataway, NJ 08854, United States, Department of Biochemistry, Robert Wood Johnson Medical School, Piscataway, NJ 08854, United States
Montelione, G.T., Dept. of Molec. Biol. and Biochem., Rutgers University, Robert Wood Johnson Medical School, Piscataway, NJ 08854, United States, Department of Biochemistry, Robert Wood Johnson Medical School, Piscataway, NJ 08854, United States
Pichersky, E., Dept. Molec., Cell., Devmtl. Biol., University of Michigan, Ann Arbor, MI 48109, United States
Klessig, D.F., Boyce Thompson Inst. for Plant Res., Tower Road, Ithaca, NY 14853, United States
Tong, L., Department of Biological Sciences, NE Structural Genomics Consortium, Columbia University, New York, NY 10027, United States
Structural and biochemical studies identify tobacco SABP2 as a methyl salicylate esterase and implicate it in plant innate immunity
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.
Scientific Publication
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