1D8V

THE RESTRAINED AND MINIMIZED AVERAGE NMR STRUCTURE OF MAP30.

Summary for 1D8V

• Entry DOI: 10.2210/pdb1d8v/pdb
• NMR Information: BMRB: 4522
• Descriptor: ANTI-HIV AND ANTI-TUMOR PROTEIN MAP30 (1 entity in total)
• Functional Keywords: single chain, antitumor protein
• Biological source: Momordica charantia (balsam pear)
• Total number of polymer chains: 1
• Total formula weight: 29630.63

Authors

Wang, Y.-X.,Neamati, N.,Jacob, J.,Palmer, I.,Stahl, S.J. (deposition date: 1999-10-26, release date: 1999-11-19, Last modification date: 2024-05-22)

Primary citation

Wang, Y.X.,Neamati, N.,Jacob, J.,Palmer, I.,Stahl, S.J.,Kaufman, J.D.,Huang, P.L.,Huang, P.L.,Winslow, H.E.,Pommier, Y.,Wingfield, P.T.,Lee-Huang, S.,Bax, A.,Torchia, D.A.
Solution structure of anti-HIV-1 and anti-tumor protein MAP30: structural insights into its multiple functions.
Cell(Cambridge,Mass.), 99:433-435, 1999

PubMed Abstract: We present the solution structure of MAP30, a plant protein with anti-HIV and anti-tumor activities. Structural analysis and subsequent biochemical assays lead to several novel discoveries. First, MAP30 acts like a DNA glycosylase/apurinic (ap) lyase, an additional activity distinct from its known RNA N-glycosidase activity toward the 28S rRNA. Glycosylase/ap lyase activity explains MAP30's apparent inhibition of the HIV-1 integrase, MAP30's ability to irreversibly relax supercoiled DNA, and may be an alternative cytotoxic pathway that contributes to MAP30's anti-HIV/anti-tumor activities. Second, two distinct, but contiguous, subsites are responsible for MAP30's glycosylase/ap lyase activity. Third, Mn2+ and Zn2+ interact with negatively charged surfaces next to the catalytic sites, facilitating DNA substrate binding instead of directly participating in catalysis.

PubMed: 10571185
DOI: 10.1016/S0092-8674(00)81529-9

Experimental method

SOLUTION NMR