2lal

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[[Image:2lal.gif|left|200px]]
 
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==CRYSTAL STRUCTURE DETERMINATION AND REFINEMENT AT 2.3 ANGSTROMS RESOLUTION OF THE LENTIL LECTIN==
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The line below this paragraph, containing "STRUCTURE_2lal", creates the "Structure Box" on the page.
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<StructureSection load='2lal' size='340' side='right'caption='[[2lal]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2lal]] 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=2LAL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LAL FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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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{{STRUCTURE_2lal| PDB=2lal | SCENE= }}
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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=2lal FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lal OCA], [https://pdbe.org/2lal PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lal RCSB], [https://www.ebi.ac.uk/pdbsum/2lal PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lal ProSAT]</span></td></tr>
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</table>
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'''CRYSTAL STRUCTURE DETERMINATION AND REFINEMENT AT 2.3 ANGSTROMS RESOLUTION OF THE LENTIL LECTIN'''
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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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==Overview==
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[[Image:Consurf_key_small.gif|200px|right]]
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We report on the X-ray structure determination of the orthorhombic crystal form of lentil lectin by molecular replacement using the pea lectin coordinates as a starting model. The structure was refined at 2.3-A resolution with a combination of molecular dynamics refinement and classical restrained least-squares refinement. The final R value for all data Fo &gt; 1 sigma (Fo) between 7.0- and 2.3-A resolution is 0.164%, and deviations from ideal bond distances are 0.014 A. The C-terminus of the beta-chain proved to be 23 amino acids longer than found in previous studies. This together with several inconsistencies between the previously determined amino acid sequence and the observed electron density forced a redetermination of the amino acid sequence of the protein. The overall structure is very similar to that of pea lectin and isolectin I of Lathyrus ochrus, the most prominent deviations being confined to loop regions and the regions of intermolecular contact. The largest difference between the pea and lentil lectin monomers is situated in the loop region of amino acids 73-79 of the beta chain. There are no significant differences between the two crystallographic independent lentil lectin monomers in the asymmetric unit. The model includes 104 well-defined water molecules, of which a significant number have a counterpart in the pea lectin structure. As for the other legume lectins, each lentil lectin monomer contains one calcium ion in a highly conserved environment. On the contrary, the manganese binding sites are distorted with respect to the pea lectin and concanavalin A structures. The Asp beta 121 side chain apparently does not ligate the Mn2+ ion. This difference is consistent in both lentil lectin monomers and agrees with earlier solution studies. Possible implications for oligosaccharide binding are discussed.
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Check<jmol>
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<jmolCheckbox>
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==About this Structure==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/la/2lal_consurf.spt"</scriptWhenChecked>
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2LAL is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Lens_culinaris Lens culinaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LAL OCA].
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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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==Reference==
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</jmolCheckbox>
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Crystal structure determination and refinement at 2.3-A resolution of the lentil lectin., Loris R, Steyaert J, Maes D, Lisgarten J, Pickersgill R, Wyns L, Biochemistry. 1993 Aug 31;32(34):8772-81. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8364026 8364026]
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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=2lal 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: Lisgarten J]]
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[[Category: Lisgarten, J.]]
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[[Category: Loris R]]
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[[Category: Loris, R.]]
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[[Category: Maes D]]
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[[Category: Maes, D.]]
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[[Category: Pickersgill R]]
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[[Category: Pickersgill, R.]]
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[[Category: Steyaert J]]
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[[Category: Steyaert, J.]]
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[[Category: Wyns L]]
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[[Category: Wyns, L.]]
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[[Category: Lectin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 09:29:36 2008''
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Current revision

CRYSTAL STRUCTURE DETERMINATION AND REFINEMENT AT 2.3 ANGSTROMS RESOLUTION OF THE LENTIL LECTIN

PDB ID 2lal

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