2bv4

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[[Image:2bv4.gif|left|200px]]<br /><applet load="2bv4" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2bv4.gif|left|200px]]
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caption="2bv4, resolution 1.00&Aring;" />
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'''1.0A STRUCTURE OF CHROMOBACTERIUM VIOLACEUM LECTIN IN COMPLEX WITH ALPHA-METHYL-MANNOSIDE'''<br />
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{{Structure
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|PDB= 2bv4 |SIZE=350|CAPTION= <scene name='initialview01'>2bv4</scene>, resolution 1.00&Aring;
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|SITE= <scene name='pdbsite=AC1:Mma+Binding+Site+For+Chain+B'>AC1</scene>
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|LIGAND= <scene name='pdbligand=MMA:O1-METHYL-MANNOSE'>MMA</scene> and <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''1.0A STRUCTURE OF CHROMOBACTERIUM VIOLACEUM LECTIN IN COMPLEX WITH ALPHA-METHYL-MANNOSIDE'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2BV4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Chromobacterium_violaceum Chromobacterium violaceum] with <scene name='pdbligand=MMA:'>MMA</scene> and <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Mma+Binding+Site+For+Chain+B'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BV4 OCA].
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2BV4 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Chromobacterium_violaceum Chromobacterium violaceum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BV4 OCA].
==Reference==
==Reference==
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Unusual entropy-driven affinity of Chromobacterium violaceum lectin CV-IIL toward fucose and mannose., Pokorna M, Cioci G, Perret S, Rebuffet E, Kostlanova N, Adam J, Gilboa-Garber N, Mitchell EP, Imberty A, Wimmerova M, Biochemistry. 2006 Jun 20;45(24):7501-10. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16768446 16768446]
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Unusual entropy-driven affinity of Chromobacterium violaceum lectin CV-IIL toward fucose and mannose., Pokorna M, Cioci G, Perret S, Rebuffet E, Kostlanova N, Adam J, Gilboa-Garber N, Mitchell EP, Imberty A, Wimmerova M, Biochemistry. 2006 Jun 20;45(24):7501-10. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16768446 16768446]
[[Category: Chromobacterium violaceum]]
[[Category: Chromobacterium violaceum]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: mannose]]
[[Category: mannose]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:41:56 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:07:05 2008''

Revision as of 14:07, 20 March 2008

Image:2bv4.gif


PDB ID 2bv4

Drag the structure with the mouse to rotate
, resolution 1.00Å
Sites:
Ligands: and
Coordinates: save as pdb, mmCIF, xml



1.0A STRUCTURE OF CHROMOBACTERIUM VIOLACEUM LECTIN IN COMPLEX WITH ALPHA-METHYL-MANNOSIDE


Overview

The purple pigmented bacterium Chromobacterium violaceum is a dominant component of tropical soil microbiota that can cause rare but fatal septicaemia in humans. Its sequenced genome provides insight into the abundant potential of this organism for biotechnological and pharmaceutical applications and allowed an ORF encoding a protein that is 60% identical to the fucose binding lectin (PA-IIL) from Pseudomonas aeruginosa and the mannose binding lectin (RS-IIL) from Ralstonia solanacearum to be identified. The lectin, CV-IIL, has recently been purified from C. violaceum [Zinger-Yosovich, K., Sudakevitz, D., Imberty, A., Garber, N. C., and Gilboa-Garber, N. (2006) Microbiology 152, 457-463] and has been confirmed to be a tetramer with subunit size of 11.86 kDa and a binding preference for fucose. We describe here the cloning of CV-IIL and its expression as a recombinant protein. A complete structure-function characterization has been made in an effort to analyze the specificity and affinity of CV-IIL for fucose and mannose. Crystal structures of CV-IIL complexes with monosaccharides have yielded the molecular basis of the specificity. Each monomer contains two close calcium cations that mediate the binding of the monosaccharides, which occurs in different orientations for fucose and mannose. The thermodynamics of binding has been analyzed by titration microcalorimetry, giving dissociation constants of 1.7 and 19 microM for alpha-methyl fucoside and alpha-methyl mannoside, respectively. Further analysis demonstrated a strongly favorable entropy term that is unusual in carbohydrate binding. A comparison with both PA-IIL and RS-IIL, which have binding preferences for fucose and mannose, respectively, yielded insights into the monosaccharide specificity of this important class of soluble bacterial lectins.

About this Structure

2BV4 is a Single protein structure of sequence from Chromobacterium violaceum. Full crystallographic information is available from OCA.

Reference

Unusual entropy-driven affinity of Chromobacterium violaceum lectin CV-IIL toward fucose and mannose., Pokorna M, Cioci G, Perret S, Rebuffet E, Kostlanova N, Adam J, Gilboa-Garber N, Mitchell EP, Imberty A, Wimmerova M, Biochemistry. 2006 Jun 20;45(24):7501-10. PMID:16768446

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