1SCR

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

1SCR の概要

• エントリーDOI: 10.2210/pdb1scr/pdb
• 分子名称: CONCANAVALIN A, NICKEL (II) ION, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: lectin(agglutinin)
• 由来する生物種: Canavalia ensiformis (jack bean)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 25721.16

構造登録者

Emmerich, C.,Helliwell, J.R.,Redshaw, M.,Naismith, J.H.,Harrop, S.J.,Raftery, J.,Kalb, A.J.,Yariv, J.,Dauter, Z.,Wilson, K.S. (登録日: 1993-12-06, 公開日: 1994-05-31, 最終更新日: 2024-02-14)

主引用文献

Emmerich, C.,Helliwell, J.R.,Redshaw, M.,Naismith, J.H.,Harrop, S.J.,Raftery, J.,Kalb, A.J.,Yariv, J.,Dauter, Z.,Wilson, K.S.
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.
Acta Crystallogr.,Sect.D, 50:749-756, 1994

PubMed Abstract: 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.

PubMed: 15299372
DOI: 10.1107/S0907444994002143

実験手法

X-RAY DIFFRACTION (2 Å)