1fat

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1fat]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Phaseolus_vulgaris Phaseolus vulgaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FAT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FAT FirstGlance]. <br>
<table><tr><td colspan='2'>[[1fat]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Phaseolus_vulgaris Phaseolus vulgaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FAT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FAT FirstGlance]. <br>
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</td></tr><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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
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<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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fat FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fat OCA], [https://pdbe.org/1fat PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fat RCSB], [https://www.ebi.ac.uk/pdbsum/1fat PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fat ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fat FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fat OCA], [https://pdbe.org/1fat PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fat RCSB], [https://www.ebi.ac.uk/pdbsum/1fat PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fat ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/PHAL_PHAVU PHAL_PHAVU]] This insecticidal carbohydrate-binding lectin is toxic for the cowpea weevil.
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[https://www.uniprot.org/uniprot/PHAL_PHAVU PHAL_PHAVU] This insecticidal carbohydrate-binding lectin is toxic for the cowpea weevil.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1fat ConSurf].
</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=1fat ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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The structure of phytohemagglutinin-L (PHA-L), a leucoagglutinating seed lectin from Phaseolus vulgaris, has been solved with molecular replacement using the coordinates of lentil lectin as model, and refined at a resolution of 2.8 A. The final R-factor of the structure is 20.0%. The quaternary structure of the PHA-L tetramer differs from the structures of the concanavalin A and peanut lectin tetramers, but resembles the structure of the soybean agglutinin tetramer. PHA-L consists of two canonical legume lectin dimers that pack together through the formation of a close contact between two beta-strands. Of the two covalently bound oligosaccharides per monomer, only one GlcNAc residue per monomer is visible in the electron density. In this article we describe the structure of PHA-L, and we discuss the putative position of the high affinity adenine-binding site present in a number of legume lectins. A comparison with transthyretin, a protein that shows a remarkable resemblance to PHA-L, gives further ground to our proposal.
 
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The crystallographic structure of phytohemagglutinin-L.,Hamelryck TW, Dao-Thi MH, Poortmans F, Chrispeels MJ, Wyns L, Loris R J Biol Chem. 1996 Aug 23;271(34):20479-85. PMID:8702788<ref>PMID:8702788</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 1fat" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
*[[Hemagglutinin 3D structures|Hemagglutinin 3D structures]]
*[[Hemagglutinin 3D structures|Hemagglutinin 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Phaseolus vulgaris]]
[[Category: Phaseolus vulgaris]]
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[[Category: Hamelryck, T]]
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[[Category: Hamelryck T]]
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[[Category: Loris, R]]
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[[Category: Loris R]]
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[[Category: Glycoprotein]]
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[[Category: Lectin]]
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[[Category: Plant defense protein]]
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Revision as of 10:12, 20 March 2024

PHYTOHEMAGGLUTININ-L

PDB ID 1fat

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