1CE3

PUTATIVE ANCESTRAL PROTEIN ENCODED BY A SINGLE SEQUENCE REPEAT OF THE MULTIDOMAIN PROTEINASE INHIBITOR FROM NICOTIANA ALATA

1CE3 の概要

• エントリーDOI: 10.2210/pdb1ce3/pdb
• NMR情報: BMRB: 4487
• 分子名称: API (1 entity in total)
• 機能のキーワード: protease inhibitor, circular permutation, nicotiana alata
• 由来する生物種: Nicotiana alata (Persian tobacco)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 5927.75

構造登録者

Scanlon, M.J.,Lee, M.C.S.,Anderson, M.A.,Craik, D.J. (登録日: 1999-03-14, 公開日: 1999-03-27, 最終更新日: 2024-10-30)

主引用文献

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

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: 10425681
DOI: 10.1016/S0969-2126(99)80103-8

実験手法

SOLUTION NMR