This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1cjp
From Proteopedia
(New page: 200px<br /><applet load="1cjp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cjp, resolution 2.78Å" /> '''CONCANAVALIN A COMPL...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1cjp.gif|left|200px]]<br /><applet load="1cjp" size=" | + | [[Image:1cjp.gif|left|200px]]<br /><applet load="1cjp" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1cjp, resolution 2.78Å" /> | caption="1cjp, resolution 2.78Å" /> | ||
'''CONCANAVALIN A COMPLEX WITH 4'-METHYLUMBELLIFERYL-ALPHA-D-GLUCOPYRANOSIDE'''<br /> | '''CONCANAVALIN A COMPLEX WITH 4'-METHYLUMBELLIFERYL-ALPHA-D-GLUCOPYRANOSIDE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Concanavalin A (Con A) is the best known plant lectin, with important | + | Concanavalin A (Con A) is the best known plant lectin, with important biological properties arising from its specific saccharide-binding ability. Its exact biological role still remains unknown. The complex of Con A with 4'-methylumbelliferyl-alpha-D-glucopyranoside (alpha-MUG) has been crystallized in space group P2(1) with cell dimensions a = 81.62 A, b = 128.71 A, c = 82.23 A, and beta = 118.47 degrees. X-ray diffraction intensities to 2.78 A have been collected. The structure of the complex was solved by molecular replacement and refined by simulated annealing methods to a crystallographic R-factor value of 0.182 and a free-R-factor value of 0.216. The asymmetric unit contains four subunits arranged as a tetramer, with approximate 222 symmetry. A saccharide molecule is bound in the sugar-binding site at the surface of each subunit, with the nonsugar (aglycon) part adopting a different orientation in each subunit. The aglycon orientation, although probably determined by packing of tetramers in the crystal lattice, helps to characterize the orientation of the saccharide in the sugar-binding pocket. The structure is the best determined alpha-D-glucoside:Con A complex to date and the hydrogen bonding network in the saccharide-binding site can be described with some confidence and compared with that of the alpha-D-mannosides. |
==About this Structure== | ==About this Structure== | ||
| - | 1CJP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Canavalia_ensiformis Canavalia ensiformis] with MUG, MN and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1CJP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Canavalia_ensiformis Canavalia ensiformis] with <scene name='pdbligand=MUG:'>MUG</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=1CJP OCA]. |
==Reference== | ==Reference== | ||
| Line 13: | Line 13: | ||
[[Category: Canavalia ensiformis]] | [[Category: Canavalia ensiformis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Hamodrakas, S | + | [[Category: Hamodrakas, S J.]] |
| - | [[Category: Kanellopoulos, P | + | [[Category: Kanellopoulos, P N.]] |
| - | [[Category: Tucker, P | + | [[Category: Tucker, P A.]] |
[[Category: CA]] | [[Category: CA]] | ||
[[Category: MN]] | [[Category: MN]] | ||
| Line 21: | Line 21: | ||
[[Category: legume lectin]] | [[Category: legume lectin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:06:43 2008'' |
Revision as of 10:06, 21 February 2008
|
CONCANAVALIN A COMPLEX WITH 4'-METHYLUMBELLIFERYL-ALPHA-D-GLUCOPYRANOSIDE
Overview
Concanavalin A (Con A) is the best known plant lectin, with important biological properties arising from its specific saccharide-binding ability. Its exact biological role still remains unknown. The complex of Con A with 4'-methylumbelliferyl-alpha-D-glucopyranoside (alpha-MUG) has been crystallized in space group P2(1) with cell dimensions a = 81.62 A, b = 128.71 A, c = 82.23 A, and beta = 118.47 degrees. X-ray diffraction intensities to 2.78 A have been collected. The structure of the complex was solved by molecular replacement and refined by simulated annealing methods to a crystallographic R-factor value of 0.182 and a free-R-factor value of 0.216. The asymmetric unit contains four subunits arranged as a tetramer, with approximate 222 symmetry. A saccharide molecule is bound in the sugar-binding site at the surface of each subunit, with the nonsugar (aglycon) part adopting a different orientation in each subunit. The aglycon orientation, although probably determined by packing of tetramers in the crystal lattice, helps to characterize the orientation of the saccharide in the sugar-binding pocket. The structure is the best determined alpha-D-glucoside:Con A complex to date and the hydrogen bonding network in the saccharide-binding site can be described with some confidence and compared with that of the alpha-D-mannosides.
About this Structure
1CJP is a Single protein structure of sequence from Canavalia ensiformis with , and as ligands. Full crystallographic information is available from OCA.
Reference
The crystal structure of the complex of concanavalin A with 4'-methylumbelliferyl-alpha-D-glucopyranoside., Hamodrakas SJ, Kanellopoulos PN, Pavlou K, Tucker PA, J Struct Biol. 1997 Feb;118(1):23-30. PMID:9087912
Page seeded by OCA on Thu Feb 21 12:06:43 2008
