1bi6

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NMR STRUCTURE OF BROMELAIN INHIBITOR VI FROM PINEAPPLE STEM

Overview

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.

About this Structure

1BI6 is a Protein complex structure of sequences from Ananas comosus. Full crystallographic information is available from OCA.

Reference

Solution structure of bromelain inhibitor IV from pineapple stem: structural similarity with Bowman-Birk trypsin/chymotrypsin inhibitor from soybean., Hatano K, Kojima M, Tanokura M, Takahashi K, Biochemistry. 1996 Apr 30;35(17):5379-84. PMID:8611527

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