2d7f: Difference between revisions

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[[Image:2d7f.gif|left|200px]]
[[Image:2d7f.gif|left|200px]]


{{Structure
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|PDB= 2d7f |SIZE=350|CAPTION= <scene name='initialview01'>2d7f</scene>, resolution 2.31&Aring;
The line below this paragraph, containing "STRUCTURE_2d7f", creates the "Structure Box" on the page.
|SITE=
You may change the PDB parameter (which sets the PDB file loaded into the applet)
|LIGAND= <scene name='pdbligand=ABA:ALPHA-AMINOBUTYRIC+ACID'>ABA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MMA:O1-METHYL-MANNOSE'>MMA</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>
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|ACTIVITY=  
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|GENE=  
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|DOMAIN=
{{STRUCTURE_2d7f| PDB=2d7f  | SCENE= }}  
|RELATEDENTRY=[[1wuv|1WUV]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2d7f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d7f OCA], [http://www.ebi.ac.uk/pdbsum/2d7f PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2d7f RCSB]</span>
}}


'''Crystal structure of A lectin from canavalia gladiata seeds complexed with alpha-methyl-mannoside and alpha-aminobutyric acid'''
'''Crystal structure of A lectin from canavalia gladiata seeds complexed with alpha-methyl-mannoside and alpha-aminobutyric acid'''
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[[Category: Sampaio, A H.]]
[[Category: Sampaio, A H.]]
[[Category: Souza, E P.]]
[[Category: Souza, E P.]]
[[Category: diocleinae]]
[[Category: Diocleinae]]
[[Category: lectin]]
[[Category: Lectin]]
[[Category: nonprotein amino acid]]
[[Category: Nonprotein amino acid]]
[[Category: plant protein]]
[[Category: Plant protein]]
 
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:30:57 2008''

Revision as of 23:48, 3 May 2008

File:2d7f.gif

Template:STRUCTURE 2d7f

Crystal structure of A lectin from canavalia gladiata seeds complexed with alpha-methyl-mannoside and alpha-aminobutyric acid


OverviewOverview

BACKGROUND: Lectins are mainly described as simple carbohydrate-binding proteins. Previous studies have tried to identify other binding sites, which possible recognize plant hormones, secondary metabolites, and isolated amino acid residues. We report the crystal structure of a lectin isolated from Canavalia gladiata seeds (CGL), describing a new binding pocket, which may be related to pathogen resistance activity in ConA-like lectins; a site where a non-protein amino-acid, alpha-aminobutyric acid (Abu), is bound. RESULTS: The overall structure of native CGL and complexed with alpha-methyl-mannoside and Abu have been refined at 2.3 A and 2.31 A resolution, respectively. Analysis of the electron density maps of the CGL structure shows clearly the presence of Abu, which was confirmed by mass spectrometry. CONCLUSION: The presence of Abu in a plant lectin structure strongly indicates the ability of lectins on carrying secondary metabolites. Comparison of the amino acids composing the site with other legume lectins revealed that this site is conserved, providing an evidence of the biological relevance of this site. This new action of lectins strengthens their role in defense mechanisms in plants.

About this StructureAbout this Structure

2D7F is a Single protein structure of sequence from Canavalia gladiata. Full crystallographic information is available from OCA.

ReferenceReference

Structure of a lectin from Canavalia gladiata seeds: new structural insights for old molecules., Delatorre P, Rocha BA, Souza EP, Oliveira TM, Bezerra GA, Moreno FB, Freitas BT, Santi-Gadelha T, Sampaio AH, Azevedo WF Jr, Cavada BS, BMC Struct Biol. 2007 Aug 2;7:52. PMID:17683532 Page seeded by OCA on Sat May 3 23:48:10 2008

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