1D6A

STRUCTURE OF POKEWEED ANTIVIRAL PROTEIN COMPLEXED WITH GUANINE

Summary for 1D6A

• Entry DOI: 10.2210/pdb1d6a/pdb
• Related: 1QCI
• Descriptor: POKEWEED ANTIVIRAL PROTEIN, GUANINE (3 entities in total)
• Functional Keywords: pokeweed antiviral protein, ribosome inactivating protein, hydrolase
• Biological source: Phytolacca americana (American pokeweed)
• Total number of polymer chains: 2
• Total formula weight: 58985.19

Authors

Kurinov, I.V.,Rajamohan, F.,Venkatachalam, T.K.,Uckun, F.M. (deposition date: 1999-10-12, release date: 1999-12-16, Last modification date: 2024-11-20)

Primary citation

Kurinov, I.V.,Rajamohan, F.,Venkatachalam, T.K.,Uckun, F.M.
X-ray crystallographic analysis of the structural basis for the interaction of pokeweed antiviral protein with guanine residues of ribosomal RNA.
Protein Sci., 8:2399-2405, 1999

PubMed Abstract: Pokeweed antiviral protein (PAP) is a ribosome-inactivating protein (RIP), which enzymatically removes a single adenine base from a conserved, surface exposed loop sequence of ribosomal rRNA. We now present unprecedented experimental evidence that PAP can release not only adenine but guanine as well from Escherichia coli rRNA, albeit at a rate 20 times slower than for adenine. We also report X-ray structure analysis and supporting modeling studies for the interactions of PAP with guanine. Our modeling studies indicated that PAP can accommodate a guanine base in the active site pocket without large conformational changes. This prediction was experimentally confirmed, since a guanine base was visible in the active site pocket of the crystal structure of the PAP-guanine complex.

PubMed: 10595542

Experimental method

X-RAY DIFFRACTION (2.1 Å)