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1uc0

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(New page: 200px<br /><applet load="1uc0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1uc0, resolution 1.85&Aring;" /> '''Crystal structure of...)
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[[Image:1uc0.jpg|left|200px]]<br /><applet load="1uc0" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1uc0, resolution 1.85&Aring;" />
 
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'''Crystal structure of wild-type hen-egg white lysozyme singly labeled with 2',3'-epoxypropyl beta-glycoside of N-acetyllactosamine'''<br />
 
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==Overview==
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==Crystal structure of wild-type hen-egg white lysozyme singly labeled with 2',3'-epoxypropyl beta-glycoside of N-acetyllactosamine==
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In spite of the belonging to the same c-type lysozyme family, hen, egg-white lysozyme (HEWL) was much less susceptible to the dual-affinity, labeling with 2',3'-epoxypropyl beta-glycoside of N-acetyllactosamine, (Galbeta1,4GlcNAc-Epo) than human lysozyme (HL). The three-dimensional, structures of the HEWL labeled with single Galbeta1,4GlcNAc-Epo and the, Glu102-mutant HL labeled with double Galbeta1,4GlcNAc-Epo were determined, by X-ray crystallography at resolutions of 1.85 and 2.0 A, respectively., The overall conformation and the interaction mode of the carbohydrate, ligand part in the singly labeled HEWL and the doubly labeled, Glu102-mutant HL were basically identical to those of the correspondingly, labeled wild-type HL with minor alterations in some stereochemical, parameters. A detailed comparison of the structures revealed the key, protein-carbohydrate and carbohydrate-carbohydrate interactions essential, for the dual labeling. It was suggested that the difference in the, efficiency of the dual labeling was caused by the structural difference, between Gln104 in HL and Asn103 in HEWL. The relevance to our previous, study and the carbohydrate-carbohydrate interaction on cell-surface, membranes were discussed.
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<StructureSection load='1uc0' size='340' side='right'caption='[[1uc0]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1uc0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UC0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UC0 FirstGlance]. <br>
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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]] 1.85&#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=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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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=1uc0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uc0 OCA], [https://pdbe.org/1uc0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uc0 RCSB], [https://www.ebi.ac.uk/pdbsum/1uc0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uc0 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/LYSC_CHICK LYSC_CHICK] Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Has bacteriolytic activity against M.luteus.<ref>PMID:22044478</ref>
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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/uc/1uc0_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=1uc0 ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1UC0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with GOL as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UC0 OCA].
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*[[Lysozyme 3D structures|Lysozyme 3D structures]]
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== References ==
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==Reference==
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<references/>
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X-ray structural analysis of the ligand-recognition mechanism in the dual-affinity labeling of c-type lysozyme with 2',3'-epoxypropyl beta-glycoside of N-acetyllactosamine., Muraki M, Harata K, J Mol Recognit. 2003 Mar-Apr;16(2):72-82. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12720276 12720276]
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__TOC__
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</StructureSection>
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
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[[Category: Lysozyme]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Harata K]]
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[[Category: Harata, K.]]
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[[Category: Muraki M]]
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[[Category: Muraki, M.]]
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[[Category: GOL]]
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[[Category: protein-carbohydrate complex]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 04:00:26 2007''
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Current revision

Crystal structure of wild-type hen-egg white lysozyme singly labeled with 2',3'-epoxypropyl beta-glycoside of N-acetyllactosamine

PDB ID 1uc0

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