1con: Difference between revisions

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New page: left|200px<br /><applet load="1con" size="450" color="white" frame="true" align="right" spinBox="true" caption="1con, resolution 2.0Å" /> '''THE REFINED STRUCTURE...
 
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[[Image:1con.gif|left|200px]]<br /><applet load="1con" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1con.gif|left|200px]]<br /><applet load="1con" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1con, resolution 2.0&Aring;" />
caption="1con, resolution 2.0&Aring;" />
'''THE REFINED STRUCTURE OF CADMIUM SUBSTITUTED CONCANAVALIN A AT 2.0 ANGSTROMS RESOLUTION'''<br />
'''THE REFINED STRUCTURE OF CADMIUM SUBSTITUTED CONCANAVALIN A AT 2.0 ANGSTROMS RESOLUTION'''<br />


==Overview==
==Overview==
The three-dimensional structure of cadmium-substituted concanavalin A has, been refined using X-PLOR. The R factor on all data between 8 and 2 A is, 17.1%. The protein crystallizes in space group I222 with cell dimensions a, = 88.7, b = 86.5 and c = 62.5 A and has one protein subunit per asymmetric, unit. The final structure contains 237 amino acids, two Cd ions, one Ca, ion and 144 water molecules. One Cd ion occupies the transition-metal, binding site and the second occupies an additional site, the coordinates, of which were first reported by Weinzierl &amp; Kalb [FEBS Lett. (1971), 18, 268-270]. The additional Cd ion is bound with distorted octahedral, symmetry and bridges the cleft between the two monomers which form the, conventional dimer of concanavalin A. This study provides a detailed, analysis of the refined structure of saccharide-free concanavalin A and is, the basis for comparison with saccharide complexes reported elsewhere.
The three-dimensional structure of cadmium-substituted concanavalin A has been refined using X-PLOR. The R factor on all data between 8 and 2 A is 17.1%. The protein crystallizes in space group I222 with cell dimensions a = 88.7, b = 86.5 and c = 62.5 A and has one protein subunit per asymmetric unit. The final structure contains 237 amino acids, two Cd ions, one Ca ion and 144 water molecules. One Cd ion occupies the transition-metal binding site and the second occupies an additional site, the coordinates of which were first reported by Weinzierl &amp; Kalb [FEBS Lett. (1971), 18, 268-270]. The additional Cd ion is bound with distorted octahedral symmetry and bridges the cleft between the two monomers which form the conventional dimer of concanavalin A. This study provides a detailed analysis of the refined structure of saccharide-free concanavalin A and is the basis for comparison with saccharide complexes reported elsewhere.


==About this Structure==
==About this Structure==
1CON is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Canavalia_ensiformis Canavalia ensiformis] with CD and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CON OCA].  
1CON is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Canavalia_ensiformis Canavalia ensiformis] with <scene name='pdbligand=CD:'>CD</scene> and <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CON OCA].  


==Reference==
==Reference==
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[[Category: Canavalia ensiformis]]
[[Category: Canavalia ensiformis]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Gilboa, A.J.Kalb.]]
[[Category: Gilboa, A J.Kalb.]]
[[Category: Habash, J.]]
[[Category: Habash, J.]]
[[Category: Harrop, S.J.]]
[[Category: Harrop, S J.]]
[[Category: Helliwell, J.R.]]
[[Category: Helliwell, J R.]]
[[Category: Hunter, W.N.]]
[[Category: Hunter, W N.]]
[[Category: Naismith, J.H.]]
[[Category: Naismith, J H.]]
[[Category: Wan, T.C.M.]]
[[Category: Wan, T C.M.]]
[[Category: Weisgerber, S.]]
[[Category: Weisgerber, S.]]
[[Category: Yariv, J.]]
[[Category: Yariv, J.]]
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[[Category: lectin(agglutinin)]]
[[Category: lectin(agglutinin)]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:37:48 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:08:07 2008''

Revision as of 13:08, 21 February 2008

File:1con.gif


1con, resolution 2.0Å

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THE REFINED STRUCTURE OF CADMIUM SUBSTITUTED CONCANAVALIN A AT 2.0 ANGSTROMS RESOLUTION

OverviewOverview

The three-dimensional structure of cadmium-substituted concanavalin A has been refined using X-PLOR. The R factor on all data between 8 and 2 A is 17.1%. The protein crystallizes in space group I222 with cell dimensions a = 88.7, b = 86.5 and c = 62.5 A and has one protein subunit per asymmetric unit. The final structure contains 237 amino acids, two Cd ions, one Ca ion and 144 water molecules. One Cd ion occupies the transition-metal binding site and the second occupies an additional site, the coordinates of which were first reported by Weinzierl & Kalb [FEBS Lett. (1971), 18, 268-270]. The additional Cd ion is bound with distorted octahedral symmetry and bridges the cleft between the two monomers which form the conventional dimer of concanavalin A. This study provides a detailed analysis of the refined structure of saccharide-free concanavalin A and is the basis for comparison with saccharide complexes reported elsewhere.

About this StructureAbout this Structure

1CON is a Single protein structure of sequence from Canavalia ensiformis with and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

Refined structure of cadmium-substituted concanavalin A at 2.0 A resolution., Naismith JH, Habash J, Harrop S, Helliwell JR, Hunter WN, Wan TC, Weisgerber S, Kalb AJ, Yariv J, Acta Crystallogr D Biol Crystallogr. 1993 Nov 1;49(Pt 6):561-71. PMID:15299493

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