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New page: left|200px<br /><applet load="1b2p" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b2p, resolution 1.7Å" /> '''NATIVE MANNOSE-SPECIF...
 
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[[Image:1b2p.gif|left|200px]]<br /><applet load="1b2p" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1b2p.gif|left|200px]]<br /><applet load="1b2p" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1b2p, resolution 1.7&Aring;" />
caption="1b2p, resolution 1.7&Aring;" />
'''NATIVE MANNOSE-SPECIFIC BULB LECTIN FROM SCILLA CAMPANULATA (BLUEBELL) AT 1.7 ANGSTROMS RESOLUTION'''<br />
'''NATIVE MANNOSE-SPECIFIC BULB LECTIN FROM SCILLA CAMPANULATA (BLUEBELL) AT 1.7 ANGSTROMS RESOLUTION'''<br />


==Overview==
==Overview==
The X-ray crystal structure of native Scilla campanulata agglutinin, a, mannose-specific lectin from bluebell bulbs and a member of the Liliaceae, family, has been determined by molecular replacement and refined to an R, value of 0.186 at 1.7 A resolution. The lectin crystallizes in space group, P21212 with unit-cell parameters a = 70. 42, b = 92.95, c = 46.64 A. The, unit cell contains eight protein molecules of Mr = 13143 Da (119, amino-acid residues). The asymmetric unit comprises two chemically, identical molecules, A and B, related by a non-crystallographic twofold, axis perpendicular to c. This dimer further associates by crystallographic, twofold symmetry to form a tetramer. The fold of the polypeptide backbone, closely resembles that found in the lectins from Galanthus nivalis, (snowdrop) and Hippeastrum (amaryllis) and contains a threefold symmetric, beta-prism made up of three antiparallel four-stranded beta-sheets. Each, of the four-stranded beta-sheets (I, II and III) possesses a potential, saccharide-binding site containing conserved residues; however, site II, has two mutations relative to sites I and III which may prevent ligation, at this site. Our study provides the first accurate and detailed, description of a native (unligated) structure from this superfamily of, mannose-specific bulb lectins and will allow comparisons with a number of, lectin-saccharide complexes which have already been determined or are, currently under investigation.
The X-ray crystal structure of native Scilla campanulata agglutinin, a mannose-specific lectin from bluebell bulbs and a member of the Liliaceae family, has been determined by molecular replacement and refined to an R value of 0.186 at 1.7 A resolution. The lectin crystallizes in space group P21212 with unit-cell parameters a = 70. 42, b = 92.95, c = 46.64 A. The unit cell contains eight protein molecules of Mr = 13143 Da (119 amino-acid residues). The asymmetric unit comprises two chemically identical molecules, A and B, related by a non-crystallographic twofold axis perpendicular to c. This dimer further associates by crystallographic twofold symmetry to form a tetramer. The fold of the polypeptide backbone closely resembles that found in the lectins from Galanthus nivalis (snowdrop) and Hippeastrum (amaryllis) and contains a threefold symmetric beta-prism made up of three antiparallel four-stranded beta-sheets. Each of the four-stranded beta-sheets (I, II and III) possesses a potential saccharide-binding site containing conserved residues; however, site II has two mutations relative to sites I and III which may prevent ligation at this site. Our study provides the first accurate and detailed description of a native (unligated) structure from this superfamily of mannose-specific bulb lectins and will allow comparisons with a number of lectin-saccharide complexes which have already been determined or are currently under investigation.


==About this Structure==
==About this Structure==
1B2P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Hyacinthoides_hispanica Hyacinthoides hispanica]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1B2P OCA].  
1B2P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Hyacinthoides_hispanica Hyacinthoides hispanica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B2P OCA].  


==Reference==
==Reference==
Line 13: Line 13:
[[Category: Hyacinthoides hispanica]]
[[Category: Hyacinthoides hispanica]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Allen, A.K.]]
[[Category: Allen, A K.]]
[[Category: Damme, E.J.M.Van.]]
[[Category: Damme, E J.M Van.]]
[[Category: Peumans, W.J.]]
[[Category: Peumans, W J.]]
[[Category: Reynolds, C.D.]]
[[Category: Reynolds, C D.]]
[[Category: Rizkallah, P.J.]]
[[Category: Rizkallah, P J.]]
[[Category: Wood, S.D.]]
[[Category: Wood, S D.]]
[[Category: Wright, L.M.]]
[[Category: Wright, L M.]]
[[Category: aglutinin]]
[[Category: aglutinin]]
[[Category: bluebell bulbs]]
[[Category: bluebell bulbs]]
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[[Category: protein- carbohydrate interactions]]
[[Category: protein- carbohydrate interactions]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 23:38:27 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:50:56 2008''

Revision as of 09:51, 21 February 2008

File:1b2p.gif


1b2p, resolution 1.7Å

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NATIVE MANNOSE-SPECIFIC BULB LECTIN FROM SCILLA CAMPANULATA (BLUEBELL) AT 1.7 ANGSTROMS RESOLUTION

Overview

The X-ray crystal structure of native Scilla campanulata agglutinin, a mannose-specific lectin from bluebell bulbs and a member of the Liliaceae family, has been determined by molecular replacement and refined to an R value of 0.186 at 1.7 A resolution. The lectin crystallizes in space group P21212 with unit-cell parameters a = 70. 42, b = 92.95, c = 46.64 A. The unit cell contains eight protein molecules of Mr = 13143 Da (119 amino-acid residues). The asymmetric unit comprises two chemically identical molecules, A and B, related by a non-crystallographic twofold axis perpendicular to c. This dimer further associates by crystallographic twofold symmetry to form a tetramer. The fold of the polypeptide backbone closely resembles that found in the lectins from Galanthus nivalis (snowdrop) and Hippeastrum (amaryllis) and contains a threefold symmetric beta-prism made up of three antiparallel four-stranded beta-sheets. Each of the four-stranded beta-sheets (I, II and III) possesses a potential saccharide-binding site containing conserved residues; however, site II has two mutations relative to sites I and III which may prevent ligation at this site. Our study provides the first accurate and detailed description of a native (unligated) structure from this superfamily of mannose-specific bulb lectins and will allow comparisons with a number of lectin-saccharide complexes which have already been determined or are currently under investigation.

About this Structure

1B2P is a Single protein structure of sequence from Hyacinthoides hispanica. Full crystallographic information is available from OCA.

Reference

Structure of the native (unligated) mannose-specific bulb lectin from Scilla campanulata (bluebell) at 1.7 A resolution., Wood SD, Wright LM, Reynolds CD, Rizkallah PJ, Allen AK, Peumans WJ, Van Damme EJ, Acta Crystallogr D Biol Crystallogr. 1999 Jul;55(Pt 7):1264-72. PMID:10393293

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