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2cav

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{{STRUCTURE_2cav| PDB=2cav | SCENE= }}
{{STRUCTURE_2cav| PDB=2cav | SCENE= }}
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'''CANAVALIN FROM JACK BEAN'''
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===CANAVALIN FROM JACK BEAN===
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==Overview==
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The structure of canavalin was refined to 2.1 and 2.0 A resolution in cubic and hexagonal crystals of space group P2(1)3 and P6(3), respectively. The threefold molecular symmetry is expressed in the symmetry of both crystals, where each identical subunit is an asymmetric unit. The canavalin subunit consists of two very similar domains, each comprised of a core subdomain having Swiss-roll topology with a loop subdomain that contains helices. The refined canavalin models resolved the discrepancy in amino-acid registers of the secondary-structural elements compared with phaseolin. The presence of strand Z in both domains of canavalin was confirmed and a new helix in the loop between strands A and B of each domain was observed. The models were analyzed in terms of the duplicated vicilin domains. Three strictly conserved residues, two glycines and a proline, were identified. The similarity between entire vicilin molecules is greater than that between separate domains of canavalin and phaseolin. Homology modeling of the sucrose-binding protein (SBP) from soybean showed a plausible trimeric assembly of subunits similar to that of vicilins.
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{{ABSTRACT_PUBMED_10739914}}
==About this Structure==
==About this Structure==
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[[Category: Swiss roll]]
[[Category: Swiss roll]]
[[Category: Vicilin]]
[[Category: Vicilin]]
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Revision as of 02:25, 29 July 2008

Image:2cav.png

Template:STRUCTURE 2cav

CANAVALIN FROM JACK BEAN

Template:ABSTRACT PUBMED 10739914

About this Structure

2CAV is a Single protein structure of sequence from Canavalia ensiformis. Full crystallographic information is available from OCA.

Reference

The refined structure of canavalin from jack bean in two crystal forms at 2.1 and 2.0 A resolution., Ko TP, Day J, McPherson A, Acta Crystallogr D Biol Crystallogr. 2000 Apr;56(Pt 4):411-20. PMID:10739914

Page seeded by OCA on Tue Jul 29 05:25:45 2008

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