1scr

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(New page: 200px<br /><applet load="1scr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1scr, resolution 2.0&Aring;" /> '''HIGH-RESOLUTION STRUC...)
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'''HIGH-RESOLUTION STRUCTURES OF SINGLE-METAL-SUBSTITUTED CONCANAVALIN A: THE CO,CA-PROTEIN AT 1.6 ANGSTROMS AND THE NI,CA-PROTEIN AT 2.0 ANGSTROMS'''<br />
'''HIGH-RESOLUTION STRUCTURES OF SINGLE-METAL-SUBSTITUTED CONCANAVALIN A: THE CO,CA-PROTEIN AT 1.6 ANGSTROMS AND THE NI,CA-PROTEIN AT 2.0 ANGSTROMS'''<br />
==Overview==
==Overview==
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The molecular structures of cobalt- and nickel-substituted concanavalin A, have been refined at 1.6 and 2.0 A resolution, respectively. Both metal, derivatives crystallize in space group I222 with approximate cell, dimensions a = 89, b = 87 and c = 63 A and one monomer in the asymmetric, unit. The final R factor for Co-substituted concanavalin A is 17.8% for 29, 211 reflections with F &gt; 1.0sigma(F) between 8.0 and 1.6 A. For, Ni-substituted concanavalin A the final R factor is 15.9% for 16 128, reflections with F &gt; 1.0sigma(F) between 8.0 and 2.0 A resolution. Both, structures contain a transition-metal binding site and a calcium-binding, site but, unlike Cd-substituted concanavalin A, do not have a third, metal-binding site. The Co-substituted concanavalin A structure diffracts, to the highest resolution of any concanavalin A structure reported to, date. A comparison of the structures of Ni-, Co-, Cd-substituted and, native concanavalin A gives an indication of coordinate errors, which is a, useful baseline for comparisons with saccharide complexes of concanavalin, A described in other work. We also give a detailed account of multiple, conformations which were found for five side-chain residues.
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The molecular structures of cobalt- and nickel-substituted concanavalin A have been refined at 1.6 and 2.0 A resolution, respectively. Both metal derivatives crystallize in space group I222 with approximate cell dimensions a = 89, b = 87 and c = 63 A and one monomer in the asymmetric unit. The final R factor for Co-substituted concanavalin A is 17.8% for 29 211 reflections with F &gt; 1.0sigma(F) between 8.0 and 1.6 A. For Ni-substituted concanavalin A the final R factor is 15.9% for 16 128 reflections with F &gt; 1.0sigma(F) between 8.0 and 2.0 A resolution. Both structures contain a transition-metal binding site and a calcium-binding site but, unlike Cd-substituted concanavalin A, do not have a third metal-binding site. The Co-substituted concanavalin A structure diffracts to the highest resolution of any concanavalin A structure reported to date. A comparison of the structures of Ni-, Co-, Cd-substituted and native concanavalin A gives an indication of coordinate errors, which is a useful baseline for comparisons with saccharide complexes of concanavalin A described in other work. We also give a detailed account of multiple conformations which were found for five side-chain residues.
==About this Structure==
==About this Structure==
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1SCR 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 NI 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=1SCR OCA].
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1SCR 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=NI:'>NI</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=1SCR OCA].
==Reference==
==Reference==
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[[Category: Dauter, Z.]]
[[Category: Dauter, Z.]]
[[Category: Emmerich, C.]]
[[Category: Emmerich, C.]]
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[[Category: Harrop, S.J.]]
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[[Category: Harrop, S J.]]
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[[Category: Helliwell, J.R.]]
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[[Category: Helliwell, J R.]]
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[[Category: Kalb, A.J.]]
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[[Category: Kalb, A J.]]
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[[Category: Naismith, J.H.]]
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[[Category: Naismith, J H.]]
[[Category: Raftery, J.]]
[[Category: Raftery, J.]]
[[Category: Redshaw, M.]]
[[Category: Redshaw, M.]]
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[[Category: Wilson, K.S.]]
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[[Category: Wilson, K S.]]
[[Category: Yariv, J.]]
[[Category: Yariv, J.]]
[[Category: CA]]
[[Category: CA]]
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[[Category: lectin(agglutinin)]]
[[Category: lectin(agglutinin)]]
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Revision as of 13:00, 21 February 2008


1scr, resolution 2.0Å

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HIGH-RESOLUTION STRUCTURES OF SINGLE-METAL-SUBSTITUTED CONCANAVALIN A: THE CO,CA-PROTEIN AT 1.6 ANGSTROMS AND THE NI,CA-PROTEIN AT 2.0 ANGSTROMS

Overview

The molecular structures of cobalt- and nickel-substituted concanavalin A have been refined at 1.6 and 2.0 A resolution, respectively. Both metal derivatives crystallize in space group I222 with approximate cell dimensions a = 89, b = 87 and c = 63 A and one monomer in the asymmetric unit. The final R factor for Co-substituted concanavalin A is 17.8% for 29 211 reflections with F > 1.0sigma(F) between 8.0 and 1.6 A. For Ni-substituted concanavalin A the final R factor is 15.9% for 16 128 reflections with F > 1.0sigma(F) between 8.0 and 2.0 A resolution. Both structures contain a transition-metal binding site and a calcium-binding site but, unlike Cd-substituted concanavalin A, do not have a third metal-binding site. The Co-substituted concanavalin A structure diffracts to the highest resolution of any concanavalin A structure reported to date. A comparison of the structures of Ni-, Co-, Cd-substituted and native concanavalin A gives an indication of coordinate errors, which is a useful baseline for comparisons with saccharide complexes of concanavalin A described in other work. We also give a detailed account of multiple conformations which were found for five side-chain residues.

About this Structure

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

Reference

High-resolution structures of single-metal-substituted concanavalin A: the Co,Ca-protein at 1.6 A and the Ni,Ca-protein at 2.0 A., Emmerich C, Helliwell JR, Redshaw M, Naismith JH, Harrop SJ, Raftery J, Kalb AJ, Yariv J, Dauter Z, Wilson KS, Acta Crystallogr D Biol Crystallogr. 1994 Sep 1;50(Pt 5):749-56. PMID:15299372

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