1CE3
PUTATIVE ANCESTRAL PROTEIN ENCODED BY A SINGLE SEQUENCE REPEAT OF THE MULTIDOMAIN PROTEINASE INHIBITOR FROM NICOTIANA ALATA
Summary for 1CE3
| Entry DOI | 10.2210/pdb1ce3/pdb |
| NMR Information | BMRB: 4487 |
| Descriptor | API (1 entity in total) |
| Functional Keywords | protease inhibitor, circular permutation, nicotiana alata |
| Biological source | Nicotiana alata (Persian tobacco) |
| Total number of polymer chains | 1 |
| Total formula weight | 5927.75 |
| Authors | Scanlon, M.J.,Lee, M.C.S.,Anderson, M.A.,Craik, D.J. (deposition date: 1999-03-14, release date: 1999-03-27, Last modification date: 2024-10-30) |
| Primary citation | Scanlon, M.J.,Lee, M.C.,Anderson, M.A.,Craik, D.J. Structure of a putative ancestral protein encoded by a single sequence repeat from a multidomain proteinase inhibitor gene from Nicotiana alata. Structure Fold.Des., 7:793-802, 1999 Cited by PubMed Abstract: The ornamental tobacco Nicotiana alata produces a series of proteinase inhibitors (PIs) that are derived from a 43 kDa precursor protein, NaProPI. NaProPI contains six highly homologous repeats that fold to generate six separate structural domains, each corresponding to one of the native PIs. An unusual feature of NaProPI is that the structural domains lie across adjacent repeats and that the sixth PI domain is generated from fragments of the first and sixth repeats. Although the homology of the repeats suggests that they may have arisen from gene duplication, the observed folding does not appear to support this. This study of the solution structure of a single NaProPI repeat (aPI1) forms a basis for unravelling the mechanism by which this protein may have evolved. PubMed: 10425681DOI: 10.1016/S0969-2126(99)80103-8 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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