1JY5

RNase-related protein from Calystegia sepium

Summary for 1JY5

• Entry DOI: 10.2210/pdb1jy5/pdb
• Descriptor: CalsepRRP (2 entities in total)
• Functional Keywords: rnase, alpha-beta protein, hydrolase
• Biological source: Calystegia sepium (hedge bindweed)
• Total number of polymer chains: 2
• Total formula weight: 46798.30

Authors

Rabijns, A.,Verboven, C.,Rouge, P.,Barre, A.,Van Damme, E.J.M.,Peumans, W.J.,De Ranter, C.J. (deposition date: 2001-09-11, release date: 2002-04-10, Last modification date: 2023-10-25)

Primary citation

Rabijns, A.,Verboven, C.,Rouge, P.,Barre, A.,Van Damme, E.J.,Peumans, W.J.,De Ranter, C.J.
Structure of an RNase-related protein from Calystegia sepium.
Acta Crystallogr.,Sect.D, 58:627-633, 2002

PubMed Abstract: 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.

PubMed: 11914487
DOI: 10.1107/S090744490200255X

Experimental method

X-RAY DIFFRACTION (2.05 Å)