Manganese and calcium binding sites of concanavalin A

Hardman, Karl D.; Agarwal, R.; Freiser, M. J.

doi:10.1016/0022-2836(82)90513-7

Cited by 177 publications

(87 citation statements)

References 34 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…However, the errors in these values at this resolution preclude detailed conclusions about the interaction of Asp l0 with calcium. It does seem clear, however, that in our structure the coordination of calcium by Aspl0 is more asymmetric than that reported previously (Hardman et al, 1982). WC is hydrogen bonded to 062 Asp208 at a distance of 2.8 A and to O Asp208, at a distance of 2.9 A. WD is hydrogen bonded to WA (cadmium ligand) at a distance of 3.2 A and to O Arg228, at a distance of 2.8 A.…”

Section: Metal Sitescontrasting

confidence: 75%

“…The ligand distances are shown in Table 7. Numbers in parentheses denote the values for manganese reported for the 1.75 ,~ structure in the paper by Hardman et al (1982). The average temperature factor of the ligands is 14 A 2 which is identical to that of the metal.…”

Section: Metal Sitesmentioning

confidence: 98%

“…The presence or absence of the cis peptide between Ala207 and Asp208 in the holo protein was resolved by Hardman et al (1982). Whether or not it is present in demetallized concanavalin A is unclear given that there are two contradictory results (Shoham et al, 1979;Reeke, Becker & Edelman, 1978).…”

Section: Confirmation Of the Cis Peptidementioning

confidence: 99%

“…The model is in excellent agreement with the difference density. This energetically unfavourable conformation is thought to be stabilized by an interaction with water 50 which interacts with the Ot52 and O of Asp208 (Hardman et al, 1982). Water 50 is ligated to the calcium ion and hence the continuing interest in whether the cis peptide is present in the demetallized structure.…”

Section: Confirmation Of the Cis Peptidementioning

confidence: 99%

See 3 more Smart Citations

Refined structure of cadmium-substituted concanavalin A at 2.0 Å resolution

Naismith¹,

Habash²,

Harrop³

et al. 1993

Acta Cryst D

View full text Add to dashboard Cite

The three-dimensional structure of cadmiumsubstituted concanavalin A has been refined using X-PLOR. The R factor on all data between 8 and 2 ,~ 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.

show abstract

Section: Metal Sitescontrasting

confidence: 75%

Section: Metal Sitesmentioning

confidence: 98%

Section: Confirmation Of the Cis Peptidementioning

confidence: 99%

Section: Confirmation Of the Cis Peptidementioning

confidence: 99%

See 2 more Smart Citations

Refined structure of cadmium-substituted concanavalin A at 2.0 Å resolution

Naismith¹,

Habash²,

Harrop³

et al. 1993

Acta Cryst D

View full text Add to dashboard Cite

show abstract

“…WD is hydrogen bonded to Arg228 O (2.8-3.0 A) and to WA (Mn 2+ ligand) (2.9-3.0/k). It is the WC interaction with Asp208 which is thought to stabilize the cis peptide (Hardman, Agarwal & Freiser, 1982).…”

Section: Metal Sitesmentioning

confidence: 99%

Refined structure of concanavalin A complexed with methyl α-D-mannopyranoside at 2.0 Å resolution and comparison with the saccharide-free structure

Naismith¹,

Emmerich²,

Habash³

et al. 1994

Acta Cryst D

152

136

View full text Add to dashboard Cite

The three-dimensional structure of the complex between methyl a-D-mannopyranoside and concanavalin A has been refined at 2.0 A resolution. Diffraction data were recorded from a single crystal (space group P21212~, a = 123.7, b = 128.6, c = 67.2 A) using synchrotron radiation at a wavelength of 1.488 A. The final model has good geometry and an R factor of 19.9% for 58871 reflections (82% complete), within the resolution limits of 8 to 2 A, with F > 1.0tr(F). The asymmetric unit contains four protein subunits arranged as a dimer of dimers with approximate 222 point symmetry. Each monomer binds one saccharide molecule. Each sugar is bound to the protein by hydrogen bonds and van der Waals contacts. Although the four subunits are not crystallographically equivalent, the protein-saccharide interactions are nearly identical in each of the four binding sites. The differences that do occur between the four sites are in the structure of the water network which surrounds each saccharide; these networks are involved in crystal packing. The structure of the complex is compared with a refined saccharide-free concanavalin A structure. The saccharide-free structure is composed of crystallographically identical subunits, again assembled as a f To whom all correspondence should be addressed.(" 1994 International Union or" Crystallography Printed in Great Britain -all rights reserved dimer of dimers, but with exact 222 symmetry. In the saccharide complex the tetramer association is different in that the monomers tend to separate resulting in fewer intersubunit interactions. The average temperature factor of the mannoside complex is considerably higher than that of the saccharide-free protein. The binding site in the saccharide-free structure is occupied by three ordered water molecules and the side chain of Asp71 from a neighbouring molecule in the crystal. These occupy positions similar to those of the four saccharide hydroxyls which are hydrogen bonded to the site. Superposition of the saccharide-binding site from each structure shows that the major changes on binding involve expulsion of these ordered solvents and the reorientation of the side chain of Tyrl00. Overall the surface accessibility of the saccharide decreases from 370 to 100 A 2 when it binds to the protein. This work builds upon the earlier studies of Derewenda et al.

show abstract

Crystallization of glycosylated and nonglycosylated phytohemagglutinin-L

et al. 1996

View full text Add to dashboard Cite

In the seeds of legume plants a class of sugar-binding proteins can be found, generally called legume lectins. In this paper we present the crystallization of phytohemagglutinin-L (PHA-L), a glycosylated lectin from the seeds of the common bean (Phaseolus vulgaris). Single PHA-L crystals were grown by vapor diffusion, using PEG as precipitant. The protein crystallizes in the monoclinic space group C2, and diffracts to a resolution of 2.7 A.The unit cell parameters are a=106.3 A, b=121.2 A, c=90.8 A, and p=93.7". The asymmetric unit probably contains one PHA-L tetramer. Crystals of a recombinant nonglycosylated form of PHA-L, grown under identical conditions, and crystals of the native PHA-L, grown in the presence of isopropanol, did not survive the mounting process.

show abstract

Manganese and calcium binding sites of concanavalin A

Cited by 177 publications

References 34 publications

Refined structure of cadmium-substituted concanavalin A at 2.0 Å resolution

Refined structure of cadmium-substituted concanavalin A at 2.0 Å resolution

Refined structure of concanavalin A complexed with methyl α-D-mannopyranoside at 2.0 Å resolution and comparison with the saccharide-free structure

Crystallization of glycosylated and nonglycosylated phytohemagglutinin-L

Contact Info

Product

Resources

About