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1len

From Proteopedia

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(New page: 200px<br /><applet load="1len" size="450" color="white" frame="true" align="right" spinBox="true" caption="1len, resolution 1.8&Aring;" /> '''REFINEMENT OF TWO CRY...)
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[[Image:1len.gif|left|200px]]<br /><applet load="1len" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1len, resolution 1.8&Aring;" />
 
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'''REFINEMENT OF TWO CRYSTAL FORMS OF LENTIL LECTIN AT 1.8 ANGSTROMS RESOLUTION'''<br />
 
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==Overview==
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==REFINEMENT OF TWO CRYSTAL FORMS OF LENTIL LECTIN AT 1.8 ANGSTROMS RESOLUTION==
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The structures of two crystal forms of lentil lectin are determined and, refined at high resolution. Orthorhombic lentil lectin is refined at 1.80, A resolution to an R-factor of 0.184 and monoclinic lentil lectin at 1.75, A resolution to an R-factor of 0.175. These two structures are compared to, each other and to the other available legume lectin structures. The, monosaccharide binding pocket of each lectin monomer contains a tightly, bound phosphate ion. This phosphate makes hydrogen bonding contacts with, Asp-81 beta, Gly-99 beta, and Asn-125 beta, three residues that are highly, conserved in most of the known legume lectin sequences and essential for, monosaccharide recognition in all legume lectin crystal structures, described thus far. A detailed analysis of the composition and properties, of the hydrophobic contact network and hydrophobic nuclei in lentil lectin, is presented. Contact map calculations reveal that dense clusters of, nonpolar as well as polar side chains play a major role in secondary, structure packing. This is illustrated by a large cluster of 24 mainly, hydrophobic amino acids that is responsible for the majority of packing, interactions between the two beta-sheets. Another series of four smaller, and less hydrophobic clusters is found to mediate the packing of a number, of loop structures upon the front sheet. A very dense, but not very, conserved cluster is found to stabilize the transition metal binding site., The highly conserved and invariant nonpolar residues are distributed, asymmetrically over the protein.
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<StructureSection load='1len' size='340' side='right'caption='[[1len]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1len]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Lens_culinaris Lens culinaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LEN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LEN FirstGlance]. <br>
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1LEN is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Lens_culinaris Lens culinaris] with PO4, MN and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LEN OCA].
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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]] 1.8&#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=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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==Reference==
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1len FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1len OCA], [https://pdbe.org/1len PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1len RCSB], [https://www.ebi.ac.uk/pdbsum/1len PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1len ProSAT]</span></td></tr>
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Structural analysis of two crystal forms of lentil lectin at 1.8 A resolution., Loris R, Van Overberge D, Dao-Thi MH, Poortmans F, Maene N, Wyns L, Proteins. 1994 Dec;20(4):330-46. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7731952 7731952]
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/LEC_LENCU LEC_LENCU] D-mannose specific lectin (By similarity).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/le/1len_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1len ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Lens culinaris]]
[[Category: Lens culinaris]]
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[[Category: Protein complex]]
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[[Category: Loris R]]
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[[Category: Loris, R.]]
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[[Category: Van Overberge D]]
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[[Category: Overberge, D.Van.]]
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[[Category: Wyns L]]
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[[Category: Wyns, L.]]
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[[Category: CA]]
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[[Category: MN]]
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[[Category: PO4]]
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[[Category: lectin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:31:18 2007''
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Current revision

REFINEMENT OF TWO CRYSTAL FORMS OF LENTIL LECTIN AT 1.8 ANGSTROMS RESOLUTION

PDB ID 1len

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