MAP30 is a 30 kDa single-stranded, type-I ribosome
inactivating protein (RIP) possessing anti-tumor and anti-HIV
activities. It binds both ribosomal RNA and the HIV-1 long-terminal
repeat DNA. To understand the structural basis for MAP30
activities, we undertook the study of MAP30 by solution
NMR spectroscopy. We report nearly complete 1H,
13C, and 15N chemical shift assignments
of its 263 amino acids. Based upon an analysis of secondary
13C chemical shifts, 3JHNHA
coupling constants, hydrogen exchange data, and nuclear
Overhauser effect patterns, we find that the secondary
structure and β-sheet topology of MAP30 are very similar
to those of the ricin A chain, a subunit of the well-known
type-II RIP, even though two proteins display distinct
activities. We therefore suggest that MAP30 and ricin A
chain share a similar three-dimensional fold, and that
the reported functional differences between two proteins
arise primarily from differences in local three-dimensional
structure and other structural properties such as surface
electrostatic potentials.