2JZ4

Putative 32 kDa myrosinase binding protein At3g16450.1 from Arabidopsis thaliana

Summary for 2JZ4

• Entry DOI: 10.2210/pdb2jz4/pdb
• NMR Information: BMRB: 15607
• Descriptor: Jasmonate inducible protein isolog (1 entity in total)
• Functional Keywords: myrosinase binding protein, at3g16450.1, sail, stereo-array isotope labeling, structural genomics, psi-2, protein structure initiative, center for eukaryotic structural genomics, cesg, unknown function
• Biological source: Arabidopsis thaliana (thale cress)
• Total number of polymer chains: 1
• Total formula weight: 31928.38

Authors

Takeda, N.,Sugimori, N.,Torizawa, T.,Terauchi, T.,Ono, A.M.,Yagi, H.,Yamaguchi, Y.,Kato, K.,Ikeya, T.,Guntert, P.,Aceti, D.J.,Markley, J.L.,Kainosho, M.,Center for Eukaryotic Structural Genomics (CESG) (deposition date: 2007-12-28, release date: 2008-02-19, Last modification date: 2024-05-08)

Primary citation

Takeda, M.,Sugimori, N.,Torizawa, T.,Terauchi, T.,Ono, A.M.,Yagi, H.,Yamaguchi, Y.,Kato, K.,Ikeya, T.,Jee, J.,Guntert, P.,Aceti, D.J.,Markley, J.L.,Kainosho, M.
Structure of the putative 32 kDa myrosinase-binding protein from Arabidopsis (At3g16450.1) determined by SAIL-NMR.
Febs J., 275:5873-5884, 2008

PubMed Abstract: The 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.

PubMed: 19021763
DOI: 10.1111/j.1742-4658.2008.06717.x

Experimental method

SOLUTION NMR