1avb

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(New page: 200px<br /><applet load="1avb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1avb, resolution 1.90&Aring;" /> '''ARCELIN-1 FROM PHASE...)
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caption="1avb, resolution 1.90&Aring;" />
caption="1avb, resolution 1.90&Aring;" />
'''ARCELIN-1 FROM PHASEOLUS VULGARIS L'''<br />
'''ARCELIN-1 FROM PHASEOLUS VULGARIS L'''<br />
==Overview==
==Overview==
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Arcelin-1 is a glycoprotein from kidney beans (Phaseolus vulgaris) which, displays insecticidal properties and protects the seeds from predation by, larvae of various bruchids. This lectin-like protein is devoid of, monosaccharide binding properties and belongs to the phytohemagglutinin, protein family. The x-ray structure determination at 1.9-A resolution of, native arcelin-1 dimers, which correspond to the functional state of the, protein in solution, was solved using multiple isomorphous replacement and, refined to a crystallographic R factor of 0.208. The three glycosylation, sites on each monomer are all covalently modified. One of these, oligosaccharide chains provides interactions with protein atoms at the, dimer interface, and another one may act by preventing the formation of, higher oligomeric species in the arcelin variants. The dimeric structure, and the severe alteration of the monosaccharide binding site in arcelin-1, correlate with the hemagglutinating properties of the protein, which are, unaffected by simple sugars and sugar derivatives. Sequence analysis and, structure comparisons of arcelin-1 with the other insecticidal proteins, from kidney beans, arcelin-5, and alpha-amylase inhibitor and with legume, lectins, yield insights into the molecular basis of the different, biological functions of these proteins.
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Arcelin-1 is a glycoprotein from kidney beans (Phaseolus vulgaris) which displays insecticidal properties and protects the seeds from predation by larvae of various bruchids. This lectin-like protein is devoid of monosaccharide binding properties and belongs to the phytohemagglutinin protein family. The x-ray structure determination at 1.9-A resolution of native arcelin-1 dimers, which correspond to the functional state of the protein in solution, was solved using multiple isomorphous replacement and refined to a crystallographic R factor of 0.208. The three glycosylation sites on each monomer are all covalently modified. One of these oligosaccharide chains provides interactions with protein atoms at the dimer interface, and another one may act by preventing the formation of higher oligomeric species in the arcelin variants. The dimeric structure and the severe alteration of the monosaccharide binding site in arcelin-1 correlate with the hemagglutinating properties of the protein, which are unaffected by simple sugars and sugar derivatives. Sequence analysis and structure comparisons of arcelin-1 with the other insecticidal proteins from kidney beans, arcelin-5, and alpha-amylase inhibitor and with legume lectins, yield insights into the molecular basis of the different biological functions of these proteins.
==About this Structure==
==About this Structure==
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1AVB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Phaseolus_vulgaris Phaseolus vulgaris] with NAG and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AVB OCA].
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1AVB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Phaseolus_vulgaris Phaseolus vulgaris] with <scene name='pdbligand=NAG:'>NAG</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AVB OCA].
==Reference==
==Reference==
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[[Category: Fabre, C.]]
[[Category: Fabre, C.]]
[[Category: Mourey, L.]]
[[Category: Mourey, L.]]
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[[Category: Pedelacq, J.D.]]
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[[Category: Pedelacq, J D.]]
[[Category: Rouge, P.]]
[[Category: Rouge, P.]]
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[[Category: Samama, J.P.]]
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[[Category: Samama, J P.]]
[[Category: NAG]]
[[Category: NAG]]
[[Category: SO4]]
[[Category: SO4]]
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[[Category: plant defense]]
[[Category: plant defense]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:09:16 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:48:37 2008''

Revision as of 09:48, 21 February 2008


1avb, resolution 1.90Å

Drag the structure with the mouse to rotate

ARCELIN-1 FROM PHASEOLUS VULGARIS L

Overview

Arcelin-1 is a glycoprotein from kidney beans (Phaseolus vulgaris) which displays insecticidal properties and protects the seeds from predation by larvae of various bruchids. This lectin-like protein is devoid of monosaccharide binding properties and belongs to the phytohemagglutinin protein family. The x-ray structure determination at 1.9-A resolution of native arcelin-1 dimers, which correspond to the functional state of the protein in solution, was solved using multiple isomorphous replacement and refined to a crystallographic R factor of 0.208. The three glycosylation sites on each monomer are all covalently modified. One of these oligosaccharide chains provides interactions with protein atoms at the dimer interface, and another one may act by preventing the formation of higher oligomeric species in the arcelin variants. The dimeric structure and the severe alteration of the monosaccharide binding site in arcelin-1 correlate with the hemagglutinating properties of the protein, which are unaffected by simple sugars and sugar derivatives. Sequence analysis and structure comparisons of arcelin-1 with the other insecticidal proteins from kidney beans, arcelin-5, and alpha-amylase inhibitor and with legume lectins, yield insights into the molecular basis of the different biological functions of these proteins.

About this Structure

1AVB is a Single protein structure of sequence from Phaseolus vulgaris with and as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of the arcelin-1 dimer from Phaseolus vulgaris at 1.9-A resolution., Mourey L, Pedelacq JD, Birck C, Fabre C, Rouge P, Samama JP, J Biol Chem. 1998 May 22;273(21):12914-22. PMID:9582323

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