5ZFO
NMR structure of IRD12 from Capsicum annum.
Summary for 5ZFO
| Entry DOI | 10.2210/pdb5zfo/pdb |
| NMR Information | BMRB: 36171 |
| Descriptor | Pin-II type proteinase inhibitor 38 (1 entity in total) |
| Functional Keywords | protein, inhibitor, capsicum annum, plant protein |
| Biological source | Capsicum annuum (Bell pepper) |
| Total number of polymer chains | 1 |
| Total formula weight | 5429.05 |
| Authors | Gartia, J.,Barnwal, R.P.,Chary, K.V.R. (deposition date: 2018-03-06, release date: 2019-05-15, Last modification date: 2024-11-06) |
| Primary citation | Gartia, J.,Anangi, R.,Joshi, R.S.,Giri, A.P.,King, G.F.,Barnwal, R.P.,Chary, K.V.R. NMR structure and dynamics of inhibitory repeat domain variant 12, a plant protease inhibitor from Capsicum annuum, and its structural relationship to other plant protease inhibitors. J.Biomol.Struct.Dyn., :1-10, 2019 Cited by PubMed Abstract: Although several plant protease inhibitors have been structurally characterized using X-ray crystallography, very few have been studied using NMR techniques. Here, we report an NMR study of the solution structure and dynamics of an inhibitory repeat domain (IRD) variant 12 from the wound-inducible Pin-II type proteinase inhibitor from . IRD variant 12 (IRD12) showed strong anti-metabolic activity against the Lepidopteran insect pest, . The NMR-derived three-dimensional structure of IRD12 reveals a three-stranded anti-parallel β-sheet rigidly held together by four disulfide bridges and shows structural homology with known IRDs. It is interesting to note that the IRD12 structure containing ∼75% unstructured part still shows substantial amount of rigidity of N-H bond vectors with respect to its molecular motion.Communicated by Ramaswamy H. Sarma. PubMed: 31038412DOI: 10.1080/07391102.2019.1607559 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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