1boi

From Proteopedia

Revision as of 12:51, 30 October 2007

N-TERMINALLY TRUNCATED RHODANESE

Overview

The NH2-terminal sequence of rhodanese influences many of its properties, ranging from mitochondrial import to folding. Rhodanese truncated by >9, residues is degraded in Escherichia coli. Mutant enzymes with lesser, truncations are recoverable and active, but they show altered active site, reactivities (Trevino, R. J., Tsalkova, T., Dramer, G., Hardesty, B., Chirgwin, J. M., and Horowitz, P. M. (1998) J. Biol. Chem. 273, 27841-27847), suggesting that the NH2-terminal sequence stabilizes the, overall structure. We tested aspects of the conformations of these, shortened species. Intrinsic and probe fluorescence showed that truncation, decreased stability and increased hydrophobic exposure, while near UV CD, suggested altered tertiary structure. Under native conditions, truncated, ... [(full description)]

About this Structure

1BOI is a [Single protein] structure of sequence from [Bos taurus]. Active as [Thiosulfate sulfurtransferase], with EC number [2.8.1.1]. Structure known Active Site: CT1. Full crystallographic information is available from [OCA].

Reference

NH2-terminal sequence truncation decreases the stability of bovine rhodanese, minimally perturbs its crystal structure, and enhances interaction with GroEL under native conditions., Trevino RJ, Gliubich F, Berni R, Cianci M, Chirgwin JM, Zanotti G, Horowitz PM, J Biol Chem. 1999 May 14;274(20):13938-47. PMID:10318804

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