The three-dimensional structure and X-ray sequence reveal that trichomaglin is a novel S-like ribonuclease.

Abstract

Trichomaglin is a protein isolated from root tuber of the plant Maganlin (Trichosanthes Lepiniate, Cucurbitaceae). The crystal structure of trichomaglin has been determined by multiple-isomorphous replacement and refined at 2.2 A resolution. The X-ray sequence was established, based on electron density combined with the experimentally determined N-terminal sequence, and the sequence information derived from mass spectroscopic analysis. X-ray sequence-based homolog search and the three-dimensional structure reveal that trichomaglin is a novel S-like RNase, which was confirmed by biological assay. Trichomaglin molecule contains an additional beta sheet in the HV(b) region, compared with the known plant RNase structures. Fourteen cystein residues form seven disulfide bridges, more than those in the other known structures of S- and S-like RNases. His43 and His105 are expected to be the catalytic acid and base, respectively. Four hydrosulfate ions are bound in the active site pocket, three of them mimicking the substrate binding sites.

Cite this paper

@article{Gan2004TheTS, title={The three-dimensional structure and X-ray sequence reveal that trichomaglin is a novel S-like ribonuclease.}, author={Jian-Hua Gan and Lu Yu and Jian Wu and Hong Xu and Joyti S Choudhary and Walter P. Blackstock and Wang-yi Liu and Z X Xia}, journal={Structure}, year={2004}, volume={12 6}, pages={1015-25} }