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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 49 561-71 (1993)
Cited: 5 times
EuropePMC logo PMID: 15299493

Abstract

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.

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Articles citing this publication (3)

  1. The 15-K neutron structure of saccharide-free concanavalin A. Blakeley MP, Kalb AJ, Helliwell JR, Myles DA. Proc Natl Acad Sci U S A 101 16405-16410 (2004)
  2. Structural analysis of two crystal forms of lentil lectin at 1.8 A resolution. Loris R, Van Overberge D, Dao-Thi MH, Poortmans F, Maene N, Wyns L. Proteins 20 330-346 (1994)
  3. High-resolution macromolecular structure determination using CCD detectors and synchrotron radiation. Walter RL, Thiel DJ, Barna SL, Tate MW, Wall ME, Eikenberry EF, Gruner SM, Ealick SE. Structure 3 835-844 (1995)


Related citations provided by authors (1)

  1. Non-Glycosylated Recombinant Pro-Concanavalin a is Active without Polypeptide Cleavage. Min W, Dunn AJ, Jones DH EMBO J. 11 1303- (1992)

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