1SGL

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

Summary for 1SGL

• Entry DOI: 10.2210/pdb1sgl/pdb
• Descriptor: trichomaglin, SULFATE ION (3 entities in total)
• Functional Keywords: trichomaglin, s-like ribonuclease, x-ray sequence, mass spectroscopic analysis, hydrolase
• Biological source: Trichosanthes lepiniana
• Total number of polymer chains: 1
• Total formula weight: 23937.09

Authors

Gan, J.-H.,Yu, L.,Wu, J.,Xu, H.,Choudhary, J.S.,Blackstock, W.P.,Liu, W.-Y.,Xia, Z.-X. (deposition date: 2004-02-24, release date: 2004-06-22, Last modification date: 2024-11-13)

Primary citation

Gan, J.H.,Yu, L.,Wu, J.,Xu, H.,Choudhary, J.S.,Blackstock, W.P.,Liu, W.Y.,Xia, Z.X.
The three-dimensional structure and X-ray sequence reveal that trichomaglin is a novel S-like ribonuclease.
Structure, 12:1015-1025, 2004

PubMed 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.

PubMed: 15274921
DOI: 10.1016/j.str.2004.03.023

Experimental method

X-RAY DIFFRACTION (2.2 Å)