2cau: Difference between revisions
New page: left|200px<br /><applet load="2cau" size="450" color="white" frame="true" align="right" spinBox="true" caption="2cau, resolution 2.1Å" /> '''CANAVALIN FROM JACK B... |
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[[Image:2cau.gif|left|200px]]<br /><applet load="2cau" size=" | [[Image:2cau.gif|left|200px]]<br /><applet load="2cau" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2cau, resolution 2.1Å" /> | caption="2cau, resolution 2.1Å" /> | ||
'''CANAVALIN FROM JACK BEAN'''<br /> | '''CANAVALIN FROM JACK BEAN'''<br /> | ||
==Overview== | ==Overview== | ||
The structure of canavalin was refined to 2.1 and 2.0 A resolution in | 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. | ||
==About this Structure== | ==About this Structure== | ||
2CAU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Canavalia_ensiformis Canavalia ensiformis]. Full crystallographic information is available from [http:// | 2CAU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Canavalia_ensiformis Canavalia ensiformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CAU OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Day, J.]] | [[Category: Day, J.]] | ||
[[Category: Ko, T | [[Category: Ko, T P.]] | ||
[[Category: Macpherson, A.]] | [[Category: Macpherson, A.]] | ||
[[Category: 7s seed protein]] | [[Category: 7s seed protein]] | ||
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[[Category: vicilin]] | [[Category: vicilin]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:46:45 2008'' | ||
Revision as of 17:46, 21 February 2008
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CANAVALIN FROM JACK BEAN
OverviewOverview
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.
About this StructureAbout this Structure
2CAU is a Single protein structure of sequence from Canavalia ensiformis. Full crystallographic information is available from OCA.
ReferenceReference
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
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