1BI6
NMR STRUCTURE OF BROMELAIN INHIBITOR VI FROM PINEAPPLE STEM
Summary for 1BI6
| Entry DOI | 10.2210/pdb1bi6/pdb |
| Descriptor | BROMELAIN INHIBITOR VI (2 entities in total) |
| Functional Keywords | cysteine protease inhibitor |
| Biological source | Ananas comosus (pineapple) More |
| Total number of polymer chains | 2 |
| Total formula weight | 5885.80 |
| Authors | Hatano, K.-I. (deposition date: 1995-12-07, release date: 1996-04-03, Last modification date: 2024-10-09) |
| Primary citation | Hatano, K.,Kojima, M.,Tanokura, M.,Takahashi, K. Solution structure of bromelain inhibitor IV from pineapple stem: structural similarity with Bowman-Birk trypsin/chymotrypsin inhibitor from soybean. Biochemistry, 35:5379-5384, 1996 Cited by PubMed Abstract: Bromelain inhibitor VI from pineapple stem (BI-VI) is a unique double-chain inhibitor with an 11-residue light chain and a 41-residue heavy chain by disulfide bonds and inhibits the cysteine proteinase bromelain competitively. The structure of BI-VI in aqueous solution was determined using nuclear magnetic resonance spectroscopy and simulated annealing-based calculations. Its three-dimensional structure was shown to be composed of two distinct domains, each of which is formed by a three-stranded antiparallel beta-sheet. Unexpectedly, BI-VI was found to share a similar folding and disulfide bond connectivities not with cystatin superfamily inhibitors which inhibit the same cysteine proteinases but with the Bowman-Birk trypsin/chymotrypsin inhibitor from soybean (BBI-I). BBI-I is a 71-residue inhibitor which has two independent inhibitory sites toward the serine proteinases trypsin and chymotrypsin. These structural similarities with BBI-I suggest that they have evolved from a common ancestor and differentiated in function during a course of molecular evolution. PubMed: 8611527DOI: 10.1021/bi952754+ PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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