1CNV

CRYSTAL STRUCTURE OF CONCANAVALIN B AT 1.65 A RESOLUTION

Summary for 1CNV

• Entry DOI: 10.2210/pdb1cnv/pdb
• Descriptor: CONCANAVALIN B (2 entities in total)
• Functional Keywords: plant chitinase, chitin binding protein, seed protein
• Biological source: Canavalia ensiformis (jack bean)
• Total number of polymer chains: 1
• Total formula weight: 33866.26

Authors

Hennig, M. (deposition date: 1995-02-20, release date: 1996-03-08, Last modification date: 2024-10-16)

Primary citation

Hennig, M.,Jansonius, J.N.,Terwisscha van Scheltinga, A.C.,Dijkstra, B.W.,Schlesier, B.
Crystal structure of concanavalin B at 1.65 A resolution. An "inactivated" chitinase from seeds of Canavalia ensiformis.
J.Mol.Biol., 254:237-246, 1995

PubMed Abstract: Seeds of Canavalia ensiformis (jack bean) contain besides large amounts of canavalin and concanavalin A, a protein with a molecular mass of 33,800 which has been named concanavalin B. Although concanavalin B shares about 40% sequence identity with plant chitinases belonging to glycosyl hydrolase family 18, no chitinase activity could be detected for this protein. To resolve this incongruity concanavalin B was crystallised and its three-dimensional structure determined at 1.65 A (1 A = 0.1 nm) resolution. The structure consists of a single domain with a (beta/alpha)8 topology. A 30 amino acid residue long loop occurs between the second beta-strand of the barrel and the second alpha-helix. This extended loop is unusual for the (beta/alpha)8 topology, but appears in a similar conformation in the structures of the seed protein narbonin and several chitinases as well. Two non-proline cis-peptide bonds are present in the structure of concanavalin B: Ser34-Phe, and Trp265-Asn. This structural feature is rarely observed in proteins, but could also be identified in the three-dimensional structures of family 18 chitinases and narbonin in coincident positions. In the chitinases the aromatic residues of the non-proline cis-peptides have been proposed to have a function in the binding of the substrate. The region in concanavalin B, where in chitinases the active site is located, shows two significant differences. First, the catalytic glutamic acid is a glutamine in concanavalin B. Second, although part of the substrate binding cleft of the chitinases is present in concanavalin B, it is much shorter. From this we conclude that concanavalin B and family 18 chitinases are closely related, but that concanavalin B has lost its enzymatic function. It still may act as a carbohydrate binding protein, however.

PubMed: 7490746
DOI: 10.1006/jmbi.1995.0614

Experimental method

X-RAY DIFFRACTION (1.65 Å)