1scr
From Proteopedia
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- | [[Image:1scr.gif|left|200px]] | + | [[Image:1scr.gif|left|200px]] |
- | + | ||
- | '''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''' | + | {{Structure |
+ | |PDB= 1scr |SIZE=350|CAPTION= <scene name='initialview01'>1scr</scene>, resolution 2.0Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene> and <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= CDNA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3823 Canavalia ensiformis]) | ||
+ | }} | ||
+ | |||
+ | '''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== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1SCR is a [ | + | 1SCR is a [[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=1SCR OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15299372 15299372] |
[[Category: Canavalia ensiformis]] | [[Category: Canavalia ensiformis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: lectin(agglutinin)]] | [[Category: lectin(agglutinin)]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:03:16 2008'' |
Revision as of 12:03, 20 March 2008
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, resolution 2.0Å | |||||||
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Ligands: | and | ||||||
Gene: | CDNA (Canavalia ensiformis) | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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. 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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