2eig: Difference between revisions

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[[Image:2eig.jpg|left|200px]]


{{Structure
==Lotus tetragonolobus seed lectin (Isoform)==
|PDB= 2eig |SIZE=350|CAPTION= <scene name='initialview01'>2eig</scene>, resolution 2.00&Aring;
<StructureSection load='2eig' size='340' side='right'caption='[[2eig]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
|SITE= <scene name='pdbsite=AC1:Nag+Binding+Site+For+Residue+A+1001'>AC1</scene>, <scene name='pdbsite=AC2:Nag+Binding+Site+For+Residue+B+3001'>AC2</scene>, <scene name='pdbsite=AC3:Mn+Binding+Site+For+Residue+A+1101'>AC3</scene>, <scene name='pdbsite=AC4:Ca+Binding+Site+For+Residue+A+1102'>AC4</scene>, <scene name='pdbsite=AC5:Mn+Binding+Site+For+Residue+B+1201'>AC5</scene>, <scene name='pdbsite=AC6:Ca+Binding+Site+For+Residue+B+1202'>AC6</scene>, <scene name='pdbsite=AC7:Mn+Binding+Site+For+Residue+C+1301'>AC7</scene>, <scene name='pdbsite=AC8:Ca+Binding+Site+For+Residue+C+1302'>AC8</scene>, <scene name='pdbsite=AC9:Mn+Binding+Site+For+Residue+D+1401'>AC9</scene> and <scene name='pdbsite=BC1:Ca+Binding+Site+For+Residue+D+1402'>BC1</scene>
== Structural highlights ==
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>
<table><tr><td colspan='2'>[[2eig]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Lotus_tetragonolobus Lotus tetragonolobus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EIG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EIG FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2eig FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2eig OCA], [https://pdbe.org/2eig PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2eig RCSB], [https://www.ebi.ac.uk/pdbsum/2eig PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2eig ProSAT]</span></td></tr>
|RELATEDENTRY=
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2eig FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2eig OCA], [http://www.ebi.ac.uk/pdbsum/2eig PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2eig RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/D0VWW1_LOTTE D0VWW1_LOTTE]
 
== Evolutionary Conservation ==
'''Lotus tetragonolobus seed lectin (Isoform)'''
[[Image:Consurf_key_small.gif|200px|right]]
 
Check<jmol>
 
  <jmolCheckbox>
==Overview==
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ei/2eig_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2eig ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Lotus tetragonolobus lectin (LTA) is a fucose-specific legume lectin. Although several studies report a diverse combination of biological activities for LTA, little is known about the mechanisms involved in l-fucosyl oligosaccharide recognition. The crystal structure of LTA at 2.0A resolution reveals a different legume lectin tetramer. Its structure consists of a homotetramer composed of two back-to-back GS4-like dimers arranged in a new mode, resulting in a novel tetramer. The LTA N-linked carbohydrate at Asn4 and the unusual LTA dimer-dimer interaction are related to its particular mode of tetramerization. In addition, we used small angle X-ray scattering to investigate the quaternary structure of LTA in solution and to compare it to the crystalline structure. Although the crystal structure of LTA has revealed a conserved metal-binding site, its l-fucose-binding site presents some punctual differences. Our investigation of the new tetramer of LTA and its fucose-binding site is essential for further studies related to cross-linking between LTA and complex divalent l-fucosyl carbohydrates.
Lotus tetragonolobus lectin (LTA) is a fucose-specific legume lectin. Although several studies report a diverse combination of biological activities for LTA, little is known about the mechanisms involved in l-fucosyl oligosaccharide recognition. The crystal structure of LTA at 2.0A resolution reveals a different legume lectin tetramer. Its structure consists of a homotetramer composed of two back-to-back GS4-like dimers arranged in a new mode, resulting in a novel tetramer. The LTA N-linked carbohydrate at Asn4 and the unusual LTA dimer-dimer interaction are related to its particular mode of tetramerization. In addition, we used small angle X-ray scattering to investigate the quaternary structure of LTA in solution and to compare it to the crystalline structure. Although the crystal structure of LTA has revealed a conserved metal-binding site, its l-fucose-binding site presents some punctual differences. Our investigation of the new tetramer of LTA and its fucose-binding site is essential for further studies related to cross-linking between LTA and complex divalent l-fucosyl carbohydrates.


==About this Structure==
Identification of a new quaternary association for legume lectins.,Moreno FB, de Oliveira TM, Martil DE, Vicoti MM, Bezerra GA, Abrego JR, Cavada BS, Filgueira de Azevedo W Jr J Struct Biol. 2008 Feb;161(2):133-43. Epub 2007 Oct 15. PMID:18068379<ref>PMID:18068379</ref>
2EIG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Lotus_tetragonolobus Lotus tetragonolobus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EIG OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Identification of a new quaternary association for legume lectins., Moreno FB, de Oliveira TM, Martil DE, Vicoti MM, Bezerra GA, Abrego JR, Cavada BS, Filgueira de Azevedo W Jr, J Struct Biol. 2008 Feb;161(2):133-43. Epub 2007 Oct 15. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18068379 18068379]
</div>
<div class="pdbe-citations 2eig" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Lotus tetragonolobus]]
[[Category: Lotus tetragonolobus]]
[[Category: Single protein]]
[[Category: Abrego JRB]]
[[Category: Abrego, J R.B.]]
[[Category: Bezerra GA]]
[[Category: Bezerra, G A.]]
[[Category: Cavada BS]]
[[Category: Cavada, B S.]]
[[Category: Filgueira de Azevedo Jr W]]
[[Category: Jr., W Filgueira de Azevedo.]]
[[Category: Moreno FBMB]]
[[Category: Moreno, F B.M B.]]
[[Category: Vicoti MM]]
[[Category: Oliveira, T M.de.]]
[[Category: De Oliveira TM]]
[[Category: Vicoti, M M.]]
[[Category: l-fucosyl]]
[[Category: lotus tetragonolobus]]
[[Category: n-acetyl-d-glucosamine]]
[[Category: sugar binding protein]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:49:35 2008''

Latest revision as of 10:53, 23 October 2024

Lotus tetragonolobus seed lectin (Isoform)Lotus tetragonolobus seed lectin (Isoform)

Structural highlights

2eig is a 4 chain structure with sequence from Lotus tetragonolobus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

D0VWW1_LOTTE

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Lotus tetragonolobus lectin (LTA) is a fucose-specific legume lectin. Although several studies report a diverse combination of biological activities for LTA, little is known about the mechanisms involved in l-fucosyl oligosaccharide recognition. The crystal structure of LTA at 2.0A resolution reveals a different legume lectin tetramer. Its structure consists of a homotetramer composed of two back-to-back GS4-like dimers arranged in a new mode, resulting in a novel tetramer. The LTA N-linked carbohydrate at Asn4 and the unusual LTA dimer-dimer interaction are related to its particular mode of tetramerization. In addition, we used small angle X-ray scattering to investigate the quaternary structure of LTA in solution and to compare it to the crystalline structure. Although the crystal structure of LTA has revealed a conserved metal-binding site, its l-fucose-binding site presents some punctual differences. Our investigation of the new tetramer of LTA and its fucose-binding site is essential for further studies related to cross-linking between LTA and complex divalent l-fucosyl carbohydrates.

Identification of a new quaternary association for legume lectins.,Moreno FB, de Oliveira TM, Martil DE, Vicoti MM, Bezerra GA, Abrego JR, Cavada BS, Filgueira de Azevedo W Jr J Struct Biol. 2008 Feb;161(2):133-43. Epub 2007 Oct 15. PMID:18068379[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Moreno FB, de Oliveira TM, Martil DE, Vicoti MM, Bezerra GA, Abrego JR, Cavada BS, Filgueira de Azevedo W Jr. Identification of a new quaternary association for legume lectins. J Struct Biol. 2008 Feb;161(2):133-43. Epub 2007 Oct 15. PMID:18068379 doi:10.1016/j.jsb.2007.10.002

2eig, resolution 2.00Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA