1BIP

BIFUNCTIONAL PROTEINASE INHIBITOR TRYPSIN/A-AMYLASE FROM SEEDS OF RAGI (ELEUSINE CORACANA GAERTNERI)

1BIP の概要

• エントリーDOI: 10.2210/pdb1bip/pdb
• 分子名称: ALPHA-AMYLASE/TRYPSIN INHIBITOR (1 entity in total)
• 機能のキーワード: serine proteinase inhibitor
• 由来する生物種: Eleusine coracana (finger millet)
• 細胞内の位置: Secreted: P01087
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13143.28

構造登録者

Strobl, S.,Muehlhahn, P.,Holak, T. (登録日: 1995-03-31, 公開日: 1995-07-10, 最終更新日: 2024-10-30)

主引用文献

Strobl, S.,Muhlhahn, P.,Bernstein, R.,Wiltscheck, R.,Maskos, K.,Wunderlich, M.,Huber, R.,Glockshuber, R.,Holak, T.A.
Determination of the three-dimensional structure of the bifunctional alpha-amylase/trypsin inhibitor from ragi seeds by NMR spectroscopy.
Biochemistry, 34:8281-8293, 1995

PubMed Abstract: The three-dimensional structure of the bifunctional alpha-amylase/trypsin inhibitor (RBI) from seeds of ragi (Eleusine coracana Gaertneri) has been determined in solution using multidimensional 1H and 15N NMR spectroscopy. The inhibitor consists of 122 amino acids, with 5 disulfide bridges, and belongs to the plant alpha-amylase/trypsin inhibitor family for which no three-dimensional structures have yet been available. The structure of the inhibitor was determined on the basis of 1131 interresidue interproton distance constraints derived from nuclear Overhauser enhancement measurements and 52 phi angles, supplemented by 9 psi and 51 chi 1 angles. RBI consists of a globular four-helix motif with a simple "up-and-down" topology. The helices are between residues 18-29, 37-51, 58-65, and 87-94. A fragment from Val 67 to Ser 69 and Gln 73 to Glu 75 forms an antiparallel beta-sheet. The fold of RBI represents a new motif among the serine proteinase inhibitors. The trypsin binding loop of RBI adopts the "canonical", substrate-like conformation which is highly conserved among serine proteinase inhibitors. The binding loop is stabilized by the two adjacent alpha-helices 1 and 2. This motif is also novel and not found in known structures of serine proteinase inhibitors. The three-dimensional structure of RBI together with biochemical data suggests the location of the alpha-amylase binding site on the face of the molecule opposite to the site of the trypsin binding loop. The RBI fold should be general for all members of the RBI family because conserved residues among the members of the family from the core of the structure.

PubMed: 7599120
DOI: 10.1021/bi00026a009

実験手法

SOLUTION NMR