Crystal structure of beta-luffin, a ribosome-inactivating protein, at 2.0 A resolution.
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.
Ma
Qing-Jun
QJ
Center for Molecular Biology, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Beijing 100101, People's Republic of China.
Li
Jian-Hui
JH
Li
Hui Guang
HG
Wu
Shen
S
Dong
Yi-Cheng
YC
D001216:Asparagine / Q000737:chemistry; D001665:Binding Sites; D018360:Crystallography, X-Ray; D004583:Electrons; D006023:Glycoproteins / Q000737:chemistry; D006860:Hydrogen Bonding; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry; D010940:Plant Proteins / Q000737:chemistry*; D010944:Plants / Q000378:metabolism; D011134:Polysaccharides / Q000737:chemistry; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D012339:RNA, Ribosomal, 28S / Q000737:chemistry; D054789:Ribosome Inactivating Proteins, Type 1; D012270:Ribosomes / Q000737:chemistry*; D015978:Trichosanthin / Q000737:chemistry
D006023:Glycoproteins; C074465:LRIP-I protein, Luffa cylindrica; D010455:Peptides; D010940:Plant Proteins; D011134:Polysaccharides; D012339:RNA, Ribosomal, 28S; D054789:Ribosome Inactivating Proteins, Type 1; C019529:polyalanine; D015978:Trichosanthin; D001216:Asparagine