Sugar binding properties of various metal ion induced conformations in concanavalin A

A. D. Sherry, A. E. Buck, C. A. Peterson

Research output: Contribution to journalArticle

22 Citations (Scopus)

Abstract

Concanavalin A is known to undergo a first-order conformational transition when metals are added to the demetallized protein at pH 5.6 (Brown, R. D., III, et al. (1977) Biochemistry 16, 3883-3896). The rate constants for this process, which we have measured using a polarographic technique, are identical when zinc, cobalt, or manganese occupies S1 and calcium occupies S2. The reducible sugar, p-nitrophenyl α-D-mannopyranoside, binds only to the locked conformational structure which is formed upon the addition of metals. The affinity of the protein for sugars is dependent upon occupancy of S1 and S2 and quite sensitive to the identity of the metal in S2. The metals may be removed from the locked protein structure and the protein temporarily retains its ability to bind with sugars but with a considerably lower affinity. The locked form of concanavalin A is unstable at a pH near 2 and unfolds to the unlocked structure with a half-life of 25 min resulting in simultaneous loss of metal and sugar binding.

Original languageEnglish (US)
Pages (from-to)2169-2173
Number of pages5
JournalBiochemistry
Volume17
Issue number11
StatePublished - 1978

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Concanavalin A
Sugars
Metal ions
Conformations
Metals
Ions
Proteins
Biochemistry
Mannose
Manganese
Cobalt
Transition metals
Zinc
Rate constants
Half-Life
Calcium

ASJC Scopus subject areas

  • Biochemistry

Cite this

Sugar binding properties of various metal ion induced conformations in concanavalin A. / Sherry, A. D.; Buck, A. E.; Peterson, C. A.

In: Biochemistry, Vol. 17, No. 11, 1978, p. 2169-2173.

Research output: Contribution to journalArticle

Sherry, A. D. ; Buck, A. E. ; Peterson, C. A. / Sugar binding properties of various metal ion induced conformations in concanavalin A. In: Biochemistry. 1978 ; Vol. 17, No. 11. pp. 2169-2173.
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