Structure-function study of maize ribosome-inactivating protein: implications for the internal inactivation region and the sole glutamate in the active site SCIE SCOPUS

Cited 28 time in WEB OF SCIENCE Cited 30 time in Scopus
Title
Structure-function study of maize ribosome-inactivating protein: implications for the internal inactivation region and the sole glutamate in the active site
Author(s)
Mak, Amanda Nga-Sze; Wong, Yuen-Ting; An, Young-Jun; Cha, Sun-Shin; Sze, Kong-Hung; Au, Shannon Wing-Ngor; Wong, Kam-Bo; Shaw, Pang-Chui
KIOST Author(s)
An, Young Jun(안영준)
Alternative Author(s)
안영준; 차선신
Publication Year
2007-09
Abstract
Maize ribosome-inactivating protein is classified as a class III or an atypical RNA N-glycosidase. It is synthesized as an inactive precursor with a 25-amino acid internal inactivation region, which is removed in the active form. As the first structural example of this class of proteins, crystals of the precursor and the active form were diffracted to 2.4 and 2.5 , respectively. The two proteins are similar, with main chain root mean square deviation (RMSD) of 0.519. In the precursor, the inactivation region is found on the protein surface and consists of a flexible loop followed by a long -helix. This region diminished both the interaction with ribosome and cytotoxicity, but not cellular uptake. Like bacterial ribosome-inactivating proteins, maize ribosome-inactivating protein does not have a back-up glutamate in the active site, which helps the protein to retain some activity if the catalytic glutamate is mutated. The structure reveals that the active site is too small to accommodate two glutamate residues. Our structure suggests that maize ribosome-inactivating protein may represent an intermediate product in the evolution of ribosome-inactivating proteins.
ISSN
0305-1048
URI
https://sciwatch.kiost.ac.kr/handle/2020.kiost/4641
DOI
10.1093/nar/gkm687
Bibliographic Citation
NUCLEIC ACIDS RESEARCH, v.35, no.18, pp.6259 - 6267, 2007
Publisher
OXFORD UNIV PRESS
Subject
POKEWEED ANTIVIRAL PROTEIN; RICIN-A-CHAIN; TRICHOSANTHIN INTERACTS; PROENZYME ACTIVATION; PLANTS; L3; EXPRESSION; RESISTANCE; RESIDUES; SAPORIN
Type
Article
Language
English
Document Type
Article
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