2OQA

X-ray Sequence and Crystal Structure of Luffaculin 1, a Novel Type 1 Ribosome-inactivating Protein

Summary for 2OQA

• Entry DOI: 10.2210/pdb2oqa/pdb
• Descriptor: Luffaculin 1, 2-acetamido-2-deoxy-beta-D-glucopyranose, TETRAETHYLENE GLYCOL, ... (5 entities in total)
• Functional Keywords: mixed alpha helix and beta sheet, hydrolase
• Biological source: Luffa acutangula
• Total number of polymer chains: 2
• Total formula weight: 53114.24

Authors

Hou, X.,Huang, M. (deposition date: 2007-01-31, release date: 2007-05-29, Last modification date: 2024-04-03)

Primary citation

Hou, X.,Chen, M.,Chen, L.,Meehan, E.J.,Xie, J.,Huang, M.
X-ray sequence and crystal structure of luffaculin 1, a novel type 1 ribosome-inactivating protein
Bmc Struct.Biol., 7:29-29, 2007

PubMed Abstract: Protein sequence can be obtained through Edman degradation, mass spectrometry, or cDNA sequencing. High resolution X-ray crystallography can also be used to derive protein sequence information, but faces the difficulty in distinguishing the Asp/Asn, Glu/Gln, and Val/Thr pairs. Luffaculin 1 is a new type 1 ribosome-inactivating protein (RIP) isolated from the seeds of Luffa acutangula. Besides rRNA N-glycosidase activity, luffaculin 1 also demonstrates activities including inhibiting tumor cells' proliferation and inducing tumor cells' differentiation.

PubMed: 17470286
DOI: 10.1186/1472-6807-7-29

Experimental method

X-RAY DIFFRACTION (1.4 Å)