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1SIY

NMR structure of mung bean non-specific lipid transfer protein 1

Summary for 1SIY
Entry DOI10.2210/pdb1siy/pdb
NMR InformationBMRB: 6089
DescriptorNonspecific lipid-transfer protein 1 (1 entity in total)
Functional Keywordsalpha helix, lipid binding protein
Biological sourceVigna radiata var. radiata (mung bean)
Total number of polymer chains1
Total formula weight9307.73
Authors
Lin, K.F.,Liu, Y.N.,Hsu, S.T.D.,Samuel, D.,Cheng, C.S.,Bonvin, A.M.J.J.,Lyu, P.C. (deposition date: 2004-03-02, release date: 2005-04-05, Last modification date: 2024-10-23)
Primary citationLin, K.F.,Liu, Y.N.,Hsu, S.T.D.,Samuel, D.,Cheng, C.S.,Bonvin, A.M.J.J.,Lyu, P.C.
Characterization and Structural Analyses of Nonspecific Lipid Transfer Protein 1 from Mung Bean
Biochemistry, 44:5703-5712, 2005
Cited by
PubMed Abstract: Plant nonspecific lipid transfer proteins (nsLTPs) are thermal stable proteins that are capable of transferring lipid molecules between bilayers in vitro. This family of proteins, abundant in plants, is proposed to be involved in defense, pollination, and germination; the in vivo biological function remains, however, elusive. Here we report the purification and sequencing of an nsLTP1 from mung bean sprouts. We have also determined the solution structure of this nsLTP1, which represents the first 3D structure of the dicotyledonous nsLTP1 family. The global fold of mung bean nsLTP1 is similar to those of the monocotyledonous nsLTP1 structures and consists of four alpha-helices stabilized by four disulfide bonds. There are, however, some notable differences in the C-terminal tails and internal hydrophobic cavities. Circular dichroism and fluorescence spectroscopy were used to compare the thermodynamics and lipid transfer properties of mung bean nsLTP1 with those of rice nsLTP1. Docking of a lipid molecule into the solution structure of mung bean nsLTP1 reveals similar binding cavities and hydrophobic interactions as in rice nsLTP1, consistent with their comparable lipid transfer properties measured experimentally.
PubMed: 15823028
DOI: 10.1021/bi047608v
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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