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Putative 32 kDa myrosinase binding protein At3g16450.1 from Arabidopsis thalianaPutative 32 kDa myrosinase binding protein At3g16450.1 from Arabidopsis thaliana
Structural highlights
FunctionJAL33_ARATH Sugar-binding protein showing significant affinity for (Glc alpha(1-4)Glc)(3) maltohexaose, (Glc alpha(1-6)Glc)(3) isomaltohexaose, Gal alpha(1-4)Gal beta(1-4)Glc, GalNAc alpha(1-3)(Fuc alpha(1-2)) and Gal beta(1-3)(Fuc alpha(1-4))GlcNAc beta(1-3)Gal beta(1-4)Glc.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe product of gene At3g16450.1 from Arabidopsis thaliana is a 32 kDa, 299-residue protein classified as resembling a myrosinase-binding protein (MyroBP). MyroBPs are found in plants as part of a complex with the glucosinolate-degrading enzyme myrosinase, and are suspected to play a role in myrosinase-dependent defense against pathogens. Many MyroBPs and MyroBP-related proteins are composed of repeated homologous sequences with unknown structure. We report here the three-dimensional structure of the At3g16450.1 protein from Arabidopsis, which consists of two tandem repeats. Because the size of the protein is larger than that amenable to high-throughput analysis by uniform (13)C/(15)N labeling methods, we used stereo-array isotope labeling (SAIL) technology to prepare an optimally (2)H/(13)C/(15)N-labeled sample. NMR data sets collected using the SAIL protein enabled us to assign (1)H, (13)C and (15)N chemical shifts to 95.5% of all atoms, even at a low concentration (0.2 mm) of protein product. We collected additional NOESY data and determined the three-dimensional structure using the cyana software package. The structure, the first for a MyroBP family member, revealed that the At3g16450.1 protein consists of two independent but similar lectin-fold domains, each composed of three beta-sheets. Structure of the putative 32 kDa myrosinase-binding protein from Arabidopsis (At3g16450.1) determined by SAIL-NMR.,Takeda M, Sugimori N, Torizawa T, Terauchi T, Ono AM, Yagi H, Yamaguchi Y, Kato K, Ikeya T, Jee J, Guntert P, Aceti DJ, Markley JL, Kainosho M FEBS J. 2008 Dec;275(23):5873-84. PMID:19021763[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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