2c4d

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[[Image:2c4d.gif|left|200px]]<br /><applet load="2c4d" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2c4d.gif|left|200px]]
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caption="2c4d, resolution 2.60&Aring;" />
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'''2.6A CRYSTAL STRUCTURE OF PSATHYRELLA VELUTINA LECTIN IN COMPLEX WITH N-ACETYLGLUCOSAMINE'''<br />
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{{Structure
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|PDB= 2c4d |SIZE=350|CAPTION= <scene name='initialview01'>2c4d</scene>, resolution 2.60&Aring;
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|SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+A'>AC1</scene>
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|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''2.6A CRYSTAL STRUCTURE OF PSATHYRELLA VELUTINA LECTIN IN COMPLEX WITH N-ACETYLGLUCOSAMINE'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2C4D is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Lacrymaria_velutina Lacrymaria velutina] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C4D OCA].
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2C4D is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Lacrymaria_velutina Lacrymaria velutina]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C4D OCA].
==Reference==
==Reference==
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Beta-propeller crystal structure of Psathyrella velutina lectin: an integrin-like fungal protein interacting with monosaccharides and calcium., Cioci G, Mitchell EP, Chazalet V, Debray H, Oscarson S, Lahmann M, Gautier C, Breton C, Perez S, Imberty A, J Mol Biol. 2006 Apr 14;357(5):1575-91. Epub 2006 Feb 6. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16497330 16497330]
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Beta-propeller crystal structure of Psathyrella velutina lectin: an integrin-like fungal protein interacting with monosaccharides and calcium., Cioci G, Mitchell EP, Chazalet V, Debray H, Oscarson S, Lahmann M, Gautier C, Breton C, Perez S, Imberty A, J Mol Biol. 2006 Apr 14;357(5):1575-91. Epub 2006 Feb 6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16497330 16497330]
[[Category: Lacrymaria velutina]]
[[Category: Lacrymaria velutina]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: psathyrella velutina]]
[[Category: psathyrella velutina]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:44:44 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:10:39 2008''

Revision as of 14:10, 20 March 2008


PDB ID 2c4d

Drag the structure with the mouse to rotate
, resolution 2.60Å
Sites:
Ligands: , and
Coordinates: save as pdb, mmCIF, xml



2.6A CRYSTAL STRUCTURE OF PSATHYRELLA VELUTINA LECTIN IN COMPLEX WITH N-ACETYLGLUCOSAMINE


Overview

The lectin from the mushroom Psathyrella velutina recognises specifically N-acetylglucosamine and N-acetylneuraminic acid containing glycans. The crystal structure of the 401 amino acid residue lectin shows that it adopts a very regular seven-bladed beta-propeller fold with the N-terminal region tucked into the central cavity around the pseudo 7-fold axis. In the complex with N-acetylglucosamine, six monosaccharides are bound in pockets located between two consecutive propeller blades. Due to the repeats shown by the sequence the binding sites are very similar. Five hydrogen bonds between the protein and the sugar hydroxyl and N-acetyl groups stabilize the complex, together with the hydrophobic interactions with a conserved tyrosine and histidine. The complex with N-acetylneuraminic acid shows molecular mimicry with the same hydrogen bond network, but with different orientations of the carbohydrate ring in the binding site. The beta-hairpin loops connecting the two inner beta-strands of each blade are metal binding sites and two to three calcium ions were located in the structure. The multispecificity and high multivalency of this mushroom lectin, combined with its similarity to the extracellular domain of an important class of cell adhesion molecules, integrins, are another example of the outstanding success of beta-propeller structures as molecular binding machines in nature.

About this Structure

2C4D is a Single protein structure of sequence from Lacrymaria velutina. Full crystallographic information is available from OCA.

Reference

Beta-propeller crystal structure of Psathyrella velutina lectin: an integrin-like fungal protein interacting with monosaccharides and calcium., Cioci G, Mitchell EP, Chazalet V, Debray H, Oscarson S, Lahmann M, Gautier C, Breton C, Perez S, Imberty A, J Mol Biol. 2006 Apr 14;357(5):1575-91. Epub 2006 Feb 6. PMID:16497330

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