1les

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(New page: 200px<br /><applet load="1les" size="450" color="white" frame="true" align="right" spinBox="true" caption="1les, resolution 1.9&Aring;" /> '''LENTIL LECTIN COMPLEX...)
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[[Image:1les.gif|left|200px]]<br /><applet load="1les" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1les, resolution 1.9&Aring;" />
caption="1les, resolution 1.9&Aring;" />
'''LENTIL LECTIN COMPLEXED WITH SUCROSE'''<br />
'''LENTIL LECTIN COMPLEXED WITH SUCROSE'''<br />
==Overview==
==Overview==
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The conformational features of sucrose in the combining site of lentil, lectin have been characterized through elucidation of a crystalline, complex at 1.9-A resolution, transferred nuclear Overhauser effect, experiments performed at 600 Mhz, and molecular modeling. In the crystal, the lentil lectin dimer binds one sucrose molecule per monomer. The, locations of 229 water molecules have been identified. NMR experiments, have provided 11 transferred NOEs. In parallel, the docking study and, conformational analysis of sucrose in the combining site of lentil lectin, indicate that three different conformations can be accommodated. Of these, the orientation with lowest energy is identical with the one observed in, the crystalline complex and provides good agreement with the observed, transferred NOEs. These structural investigations indicate that the bound, sucrose has a unique conformation for the glycosidic linkage, close to the, one observed in crystalline sucrose, whereas the fructofuranose ring, remains relatively flexible and does not exhibit any strong interaction, with the protein. Major differences in the hydrogen bonding network of, sucrose are found. None of the two inter-residue hydrogen bonds in, crystalline sucrose are conserved in the complex with the lectin. Instead, a water molecule bridges hydroxyl groups O2-g and O3-f of sucrose.
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The conformational features of sucrose in the combining site of lentil lectin have been characterized through elucidation of a crystalline complex at 1.9-A resolution, transferred nuclear Overhauser effect experiments performed at 600 Mhz, and molecular modeling. In the crystal, the lentil lectin dimer binds one sucrose molecule per monomer. The locations of 229 water molecules have been identified. NMR experiments have provided 11 transferred NOEs. In parallel, the docking study and conformational analysis of sucrose in the combining site of lentil lectin indicate that three different conformations can be accommodated. Of these, the orientation with lowest energy is identical with the one observed in the crystalline complex and provides good agreement with the observed transferred NOEs. These structural investigations indicate that the bound sucrose has a unique conformation for the glycosidic linkage, close to the one observed in crystalline sucrose, whereas the fructofuranose ring remains relatively flexible and does not exhibit any strong interaction with the protein. Major differences in the hydrogen bonding network of sucrose are found. None of the two inter-residue hydrogen bonds in crystalline sucrose are conserved in the complex with the lectin. Instead, a water molecule bridges hydroxyl groups O2-g and O3-f of sucrose.
==About this Structure==
==About this Structure==
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1LES is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Lens_culinaris Lens culinaris] with CA and MN as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LES OCA].
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1LES is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Lens_culinaris Lens culinaris] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=MN:'>MN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LES OCA].
==Reference==
==Reference==
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[[Category: protein-sugar interactions]]
[[Category: protein-sugar interactions]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:31:31 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:44:20 2008''

Revision as of 11:44, 21 February 2008


1les, resolution 1.9Å

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LENTIL LECTIN COMPLEXED WITH SUCROSE

Overview

The conformational features of sucrose in the combining site of lentil lectin have been characterized through elucidation of a crystalline complex at 1.9-A resolution, transferred nuclear Overhauser effect experiments performed at 600 Mhz, and molecular modeling. In the crystal, the lentil lectin dimer binds one sucrose molecule per monomer. The locations of 229 water molecules have been identified. NMR experiments have provided 11 transferred NOEs. In parallel, the docking study and conformational analysis of sucrose in the combining site of lentil lectin indicate that three different conformations can be accommodated. Of these, the orientation with lowest energy is identical with the one observed in the crystalline complex and provides good agreement with the observed transferred NOEs. These structural investigations indicate that the bound sucrose has a unique conformation for the glycosidic linkage, close to the one observed in crystalline sucrose, whereas the fructofuranose ring remains relatively flexible and does not exhibit any strong interaction with the protein. Major differences in the hydrogen bonding network of sucrose are found. None of the two inter-residue hydrogen bonds in crystalline sucrose are conserved in the complex with the lectin. Instead, a water molecule bridges hydroxyl groups O2-g and O3-f of sucrose.

About this Structure

1LES is a Protein complex structure of sequences from Lens culinaris with and as ligands. Full crystallographic information is available from OCA.

Reference

NMR, molecular modeling, and crystallographic studies of lentil lectin-sucrose interaction., Casset F, Hamelryck T, Loris R, Brisson JR, Tellier C, Dao-Thi MH, Wyns L, Poortmans F, Perez S, Imberty A, J Biol Chem. 1995 Oct 27;270(43):25619-28. PMID:7592736

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