1rin
From Proteopedia
(New page: 200px<br /><applet load="1rin" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rin, resolution 2.6Å" /> '''X-RAY CRYSTAL STRUCTU...) |
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| - | [[Image:1rin.gif|left|200px]]<br /><applet load="1rin" size=" | + | [[Image:1rin.gif|left|200px]]<br /><applet load="1rin" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1rin, resolution 2.6Å" /> | caption="1rin, resolution 2.6Å" /> | ||
'''X-RAY CRYSTAL STRUCTURE OF A PEA LECTIN-TRIMANNOSIDE COMPLEX AT 2.6 ANGSTROMS RESOLUTION'''<br /> | '''X-RAY CRYSTAL STRUCTURE OF A PEA LECTIN-TRIMANNOSIDE COMPLEX AT 2.6 ANGSTROMS RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The x-ray crystal structure of pea lectin, in complex with a methyl | + | The x-ray crystal structure of pea lectin, in complex with a methyl glycoside of the N-linked-type oligosaccharide trimannosyl core, methyl 3,6-di-O-(alpha-D-mannopyranosyl)-alpha-D-mannopyranoside, has been solved by molecular replacement and refined at 2.6-A resolution. The R factor is 0.183 for all data in the 8.0 to 2.6 A resolution range with an average atomic temperature factor of 26.1 A2. Strong electron density for a single mannose residue is found in the monosaccharide-binding site suggesting that the trisaccharide binds primarily through one of the terminal alpha-linked mannose residues. The complex is stabilized by hydrogen bonds involving the protein residues Asp-81, Gly-99, Asn-125, Ala-217, and Glu-218, and the carbohydrate oxygen atoms O3, O4, O5, and O6. In addition, the carbohydrate makes van der Waals contacts with the protein, involving Phe-123 in particular. These interactions are very similar to those found in the monosaccharide complexes with concanavalin A and isolectin 1 of Lathyrus ochrus, confirming the structural relatedness of this family of proteins. Comparison of the pea lectin complex with the unliganded pea lectin and concanavalin A structures indicates differences in the conformation and water structure of the unliganded binding sites of these two proteins. Furthermore, a correlation between the position of the carbohydrate oxygen atoms in the complex and the bound water molecules in the unliganded binding sites is found. Binding of the trimannose core through a single terminal monosaccharide residue strongly argues that an additional fucose-binding site is responsible for the high affinity pea lectin-oligosaccharide interactions. |
==About this Structure== | ==About this Structure== | ||
| - | 1RIN is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum] with MAN, MN and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1RIN is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum] with <scene name='pdbligand=MAN:'>MAN</scene>, <scene name='pdbligand=MN:'>MN</scene> and <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RIN OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Pisum sativum]] | [[Category: Pisum sativum]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Carver, J | + | [[Category: Carver, J P.]] |
[[Category: Einspahr, H.]] | [[Category: Einspahr, H.]] | ||
| - | [[Category: Hardman, K | + | [[Category: Hardman, K D.]] |
| - | [[Category: Rini, J | + | [[Category: Rini, J M.]] |
| - | [[Category: Suddath, F | + | [[Category: Suddath, F L.]] |
[[Category: CA]] | [[Category: CA]] | ||
[[Category: MAN]] | [[Category: MAN]] | ||
| Line 23: | Line 23: | ||
[[Category: lectin]] | [[Category: lectin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:51:15 2008'' |
Revision as of 12:51, 21 February 2008
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X-RAY CRYSTAL STRUCTURE OF A PEA LECTIN-TRIMANNOSIDE COMPLEX AT 2.6 ANGSTROMS RESOLUTION
Overview
The x-ray crystal structure of pea lectin, in complex with a methyl glycoside of the N-linked-type oligosaccharide trimannosyl core, methyl 3,6-di-O-(alpha-D-mannopyranosyl)-alpha-D-mannopyranoside, has been solved by molecular replacement and refined at 2.6-A resolution. The R factor is 0.183 for all data in the 8.0 to 2.6 A resolution range with an average atomic temperature factor of 26.1 A2. Strong electron density for a single mannose residue is found in the monosaccharide-binding site suggesting that the trisaccharide binds primarily through one of the terminal alpha-linked mannose residues. The complex is stabilized by hydrogen bonds involving the protein residues Asp-81, Gly-99, Asn-125, Ala-217, and Glu-218, and the carbohydrate oxygen atoms O3, O4, O5, and O6. In addition, the carbohydrate makes van der Waals contacts with the protein, involving Phe-123 in particular. These interactions are very similar to those found in the monosaccharide complexes with concanavalin A and isolectin 1 of Lathyrus ochrus, confirming the structural relatedness of this family of proteins. Comparison of the pea lectin complex with the unliganded pea lectin and concanavalin A structures indicates differences in the conformation and water structure of the unliganded binding sites of these two proteins. Furthermore, a correlation between the position of the carbohydrate oxygen atoms in the complex and the bound water molecules in the unliganded binding sites is found. Binding of the trimannose core through a single terminal monosaccharide residue strongly argues that an additional fucose-binding site is responsible for the high affinity pea lectin-oligosaccharide interactions.
About this Structure
1RIN is a Protein complex structure of sequences from Pisum sativum with , and as ligands. Full crystallographic information is available from OCA.
Reference
X-ray crystal structure of a pea lectin-trimannoside complex at 2.6 A resolution., Rini JM, Hardman KD, Einspahr H, Suddath FL, Carver JP, J Biol Chem. 1993 May 15;268(14):10126-32. PMID:8486683
Page seeded by OCA on Thu Feb 21 14:51:15 2008
Categories: Pisum sativum | Protein complex | Carver, J P. | Einspahr, H. | Hardman, K D. | Rini, J M. | Suddath, F L. | CA | MAN | MN | Lectin
