1d6a
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /><applet load="1d6a" size="450" color="white" frame="true" align="right" spinBox="true" caption="1d6a, resolution 2.1Å" /> '''STRUCTURE OF POKEWEED...)
Next diff →
Revision as of 10:54, 20 November 2007
|
STRUCTURE OF POKEWEED ANTIVIRAL PROTEIN COMPLEXED WITH GUANINE
Overview
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.
About this Structure
1D6A is a Single protein structure of sequence from Phytolacca americana with GUN as ligand. Active as rRNA N-glycosylase, with EC number 3.2.2.22 Full crystallographic information is available from OCA.
Reference
X-ray crystallographic analysis of the structural basis for the interaction of pokeweed antiviral protein with guanine residues of ribosomal RNA., Kurinov IV, Rajamohan F, Venkatachalam TK, Uckun FM, Protein Sci. 1999 Nov;8(11):2399-405. PMID:10595542
Page seeded by OCA on Tue Nov 20 13:02:06 2007
