1NIO

Crystal structure of beta-luffin, a ribosome inactivating protein at 2.0A resolution

Summary for 1NIO

• Entry DOI: 10.2210/pdb1nio/pdb
• Descriptor: b-luffin, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• Functional Keywords: ribosome inactivating protein(rip), beta-luffin, hydrolase
• Biological source: Luffa aegyptiaca (smooth loofah)
• Total number of polymer chains: 1
• Total formula weight: 27767.63

Authors

Wu, S. (deposition date: 2002-12-24, release date: 2003-08-05, Last modification date: 2024-10-30)

Primary citation

Ma, Q.J.,Li, J.H.,Li, H.G.,Wu, S.,Dong, Y.C.
Crystal structure of beta-luffin, a ribosome-inactivating protein, at 2.0 A resolution.
Acta Crystallogr.,Sect.D, 59:1366-1370, 2003

PubMed Abstract: The crystal structure of beta-luffin at 2.0 A resolution was solved by the molecular-replacement method using polyalanyl trichosanthin as the search model. The structure was refined with CNS1.1, giving R(work) = 0.162 and R(free) = 0.204. The r.m.s.d.s of the bond lengths and bond angles are 0.008 A and 1.3 degrees, respectively. The overall structure is similar to those of other type I RIPs. Three N-acetylglucosamine (Nag) molecules are linked to residues Asn2, Asn78 and Asn85 of the protein.

PubMed: 12876337
DOI: 10.1107/S0907444903011156

Experimental method

X-RAY DIFFRACTION (2 Å)