Abstract

The binding of Mn to apo lectins is required for their biological functionas carbohydrate-binding proteins. A previous ESEEM study of the Mn site of the lectin from Conavalia ensiformis (Con A) not only demonstrated histidine ligation, but also water ligands that were not resolved in the crystal structure of Con A. Lectins from Dioclea, like those from Conavalia, also binds carbohydrates with high specificity, but with a very different G. A crystal structure of a Dioclea lectin shows an identical carbohydrate-binding site to that of Con A. The difference in the thermodynamics of carbohydrate-binding of the two classes of lectins may be the result of difference in solvent packing that is not resolved in the crystal structure. EPR of five Dioclea lectins (D. rostrata, D. guianensis, D. violacea, D. virgata, D. grandiflora) and one from Cratylia floribunda are compared to those from Conavalia (C. brasiliensis, C. bonariensis and C. ensiformis [Con A]). All except D. rostrata and Cratylia floribunda, exhibit an EPR spectrum similar to that of Con A. ESEEM studies are being conducted to examine the Mn site of these lectins and compared to that of Con A in order to investigate the possibility that difference in water ligation plays a role in the different thermodynamics of carbohydrate-binding of the two classes of lectins.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR002583-13
Application #
6281733
Study Section
Project Start
1998-05-05
Project End
2000-04-30
Budget Start
1997-10-01
Budget End
1998-09-30
Support Year
13
Fiscal Year
1998
Total Cost
Indirect Cost

  Institution

Name
Albert Einstein College of Medicine
Department
Type
DUNS #
009095365
City
Bronx
State
NY
Country
United States
Zip Code
10461

  Publications

Colaneri, M J; Vitali, J; Peisach, J (2000) Electron spin-echo envelope modulation study of multicrystalline Cu(2+)-insulin: effects of Cd(2+) on the nuclear quadrupole interaction of the Cu(2+)-coordinated imidazole remote nitrogen. Biochemistry 39:584-91
Lee, H C; Goroncy, A K; Peisach, J et al. (2000) Demonstration of a conserved histidine and two water ligands at the Mn2+ site in Diocleinae lectins by pulsed EPR spectroscopy. Biochemistry 39:2340-6
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Magliozzo, R S; Marcinkeviciene, J A (1997) The role of Mn(II)-peroxidase activity of mycobacterial catalase-peroxidase in activation of the antibiotic isoniazid. J Biol Chem 272:8867-70
Nersissian, A M; Mehrabian, Z B; Nalbandyan, R M et al. (1996) Cloning, expression, and spectroscopic characterization of Cucumis sativus stellacyanin in its nonglycosylated form. Protein Sci 5:2184-92
Gasdaska, J R; Law, J H; Bender, C J et al. (1996) Cockroach transferrin closely resembles vertebrate transferrins in its metal ion-binding properties: a spectroscopic study. J Inorg Biochem 64:247-58
Tipton, P A; Quinn, T P; Peisach, J et al. (1996) Role of the divalent metal ion in the NAD:malic enzyme reaction: an ESEEM determination of the ground state conformation of malate in the E:Mn:malate complex. Protein Sci 5:1648-54
Coffino, A R; Peisach, J (1996) Simulation of Mn (II) EPR spectra using a full spin-Hamiltonian approach. J Magn Reson B 111:127-34
Parast, C V; Wong, K K; Lewisch, S A et al. (1995) Hydrogen exchange of the glycyl radical of pyruvate formate-lyase is catalyzed by cysteine 419. Biochemistry 34:2393-9
Theodorakis, J L; Garber, E A; McCracken, J et al. (1995) A chemical modification of cytochrome-c lysines leading to changes in heme iron ligation. Biochim Biophys Acta 1252:103-13

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