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 Å and an R factor of 20.74%. Although the protein is completely devoid of ribonuclease activity, it adopts the typical α + β structu...

Full description

Saved in:
Bibliographic Details
Published in:Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2002-04, Vol.58 (4), p.627-633
Main Authors: Rabijns, A., Verboven, C., Rougé, P., Barre, A., Van Damme, E. J. M., Peumans, W. J., De Ranter, C. J.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Binding Sites
Crystallography, X-Ray
Models, Molecular
Molecular Sequence Data
Plant Proteins - chemistry
Protein Structure, Secondary
ribonuclease
Sequence Alignment
storage protein
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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 Å and an R factor of 20.74%. Although the protein is completely devoid of ribonuclease activity, it adopts the typical α + β 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.
ISSN:1399-0047
0907-4449
1399-0047
DOI:10.1107/S090744490200255X