Structure of an RNase-related protein from Calystegia sepium.
The structure of a catalytically inactive RNase-related protein from Calystegia sepium (CalsepRRP) has been resolved by protein crystallography at a resolution of 2.05 A and an R factor of 20.74%. Although the protein is completely devoid of ribonuclease activity, it adopts the typical alpha + beta structure of non-base-specific RNases. Analysis of the structure revealed that two amino-acid substitutions in the 'active' P1 site, in combination with the less hydrophobic/aromatic character of the B1 base-recognition site and a completely disrupted B2 base-recognition site, might account for this complete lack of activity.
Rabijns
A
A
Laboratory of Analytical Chemistry and Medicinal Physicochemistry, Faculty of Pharmaceutical Sciences, K. U. Leuven, E. Van Evenstraat 4, B-3000 Leuven, Belgium.
Verboven
C
C
Rougé
P
P
Barre
A
A
Van Damme
E J M
EJ
Peumans
W J
WJ
De Ranter
C J
CJ
D000595:Amino Acid Sequence; D001665:Binding Sites; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000737:chemistry*; D017433:Protein Structure, Secondary; D016415:Sequence Alignment
D010940:Plant Proteins; C405543:RNase-related protein, Calystegia sepium