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1cnv
From Proteopedia
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'''CRYSTAL STRUCTURE OF CONCANAVALIN B AT 1.65 A RESOLUTION''' | '''CRYSTAL STRUCTURE OF CONCANAVALIN B AT 1.65 A RESOLUTION''' | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Hennig, M.]] | [[Category: Hennig, M.]] | ||
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| - | [[Category: | + | [[Category: Plant chitinase]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:55:54 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 09:55, 2 May 2008
CRYSTAL STRUCTURE OF CONCANAVALIN B AT 1.65 A RESOLUTION
Overview
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.
About this Structure
1CNV is a Single protein structure of sequence from Canavalia ensiformis. Full crystallographic information is available from OCA.
Reference
Crystal structure of concanavalin B at 1.65 A resolution. An "inactivated" chitinase from seeds of Canavalia ensiformis., Hennig M, Jansonius JN, Terwisscha van Scheltinga AC, Dijkstra BW, Schlesier B, J Mol Biol. 1995 Nov 24;254(2):237-46. PMID:7490746 Page seeded by OCA on Fri May 2 12:55:54 2008
