2cy6
From Proteopedia
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|PDB= 2cy6 |SIZE=350|CAPTION= <scene name='initialview01'>2cy6</scene>, resolution 2.00Å | |PDB= 2cy6 |SIZE=350|CAPTION= <scene name='initialview01'>2cy6</scene>, resolution 2.00Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=TRE:TREHALOSE'>TRE</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2cwm|2CWM]], [[2cyf|2CYF]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2cy6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cy6 OCA], [http://www.ebi.ac.uk/pdbsum/2cy6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2cy6 RCSB]</span> | ||
}} | }} | ||
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[[Category: Rocha, B A.M.]] | [[Category: Rocha, B A.M.]] | ||
[[Category: Souza, E P.]] | [[Category: Souza, E P.]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: MN]] | ||
| - | [[Category: TRE]] | ||
[[Category: canavalia maritima]] | [[Category: canavalia maritima]] | ||
[[Category: lectin]] | [[Category: lectin]] | ||
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[[Category: x-ray diffraction]] | [[Category: x-ray diffraction]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:27:55 2008'' |
Revision as of 23:27, 30 March 2008
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| , resolution 2.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Related: | 2CWM, 2CYF
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of ConM in complex with trehalose and maltose
Overview
The crystal structure of Canavalia maritima lectin (ConM) complexed with trehalose and maltose revealed relevant point mutations in ConA-like lectins. ConM with the disaccharides and other ConA-like lectins complexed with carbohydrates demonstrated significant differences in the position of H-bonds. The main difference in the ConM structure is the replacement of Pro202 by Ser202, a residue that promotes the approximation of Tyr12 to the carbohydrate-binding site. The O-6' of the second glucose ring in maltose interacts with Tyr12, while in trehalose the interaction is established by the O-2' and Tyr12, explaining the higher affinity of ConM for disaccharides compared to monosaccharides.
About this Structure
2CY6 is a Protein complex structure of sequences from Canavalia maritima. Full crystallographic information is available from OCA.
Reference
Crystal structure of a lectin from Canavalia maritima (ConM) in complex with trehalose and maltose reveals relevant mutation in ConA-like lectins., Delatorre P, Rocha BA, Gadelha CA, Santi-Gadelha T, Cajazeiras JB, Souza EP, Nascimento KS, Freire VN, Sampaio AH, Azevedo WF Jr, Cavada BS, J Struct Biol. 2006 Jun;154(3):280-6. Epub 2006 Apr 21. PMID:16677825
Page seeded by OCA on Mon Mar 31 02:27:55 2008
