X-ray sequence and crystal structure of luffaculin 1, a novel type 1 ribosome-inactivating protein.

ABSTRACT:

Background

Protein sequence can be obtained through Edman degradation, mass spectrometry, or cDNA sequencing. High resolution X-ray crystallography can also be used to derive protein sequence information, but faces the difficulty in distinguishing the Asp/Asn, Glu/Gln, and Val/Thr pairs. Luffaculin 1 is a new type 1 ribosome-inactivating protein (RIP) isolated from the seeds of Luffa acutangula. Besides rRNA N-glycosidase activity, luffaculin 1 also demonstrates activities including inhibiting tumor cells' proliferation and inducing tumor cells' differentiation.

Results

The crystal structure of luffaculin 1 was determined at 1.4 A resolution. Its amino-acid sequence was derived from this high resolution structure using the following criteria: 1) high resolution electron dens

SUBMITTER: Hou X 

PROVIDER: S-EPMC1868734 | biostudies-literature | 2007 Apr

REPOSITORIES: biostudies-literature