Structural highlights
Function
Q9M7C7_CALSE
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Structure of an RNase-related protein from Calystegia sepium.,Rabijns A, Verboven C, Rouge P, Barre A, Van Damme EJ, Peumans WJ, De Ranter CJ Acta Crystallogr D Biol Crystallogr. 2002 Apr;58(Pt 4):627-33. Epub 2002, Mar 22. PMID:11914487[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Rabijns A, Verboven C, Rouge P, Barre A, Van Damme EJ, Peumans WJ, De Ranter CJ. Structure of an RNase-related protein from Calystegia sepium. Acta Crystallogr D Biol Crystallogr. 2002 Apr;58(Pt 4):627-33. Epub 2002, Mar 22. PMID:11914487