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1scr
From Proteopedia
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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 NI and CA 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
Page seeded by OCA on Wed Nov 21 02:16:52 2007
