1jef

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(New page: 200px<br /><applet load="1jef" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jef, resolution 1.77&Aring;" /> '''TURKEY LYSOZYME COMP...)
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[[Image:1jef.gif|left|200px]]<br /><applet load="1jef" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1jef, resolution 1.77&Aring;" />
 
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'''TURKEY LYSOZYME COMPLEX WITH (GLCNAC)3'''<br />
 
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==Overview==
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==TURKEY LYSOZYME COMPLEX WITH (GLCNAC)3==
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The turkey-egg lysozyme (TEL) complex with tri-N-acetylchitotriose, [(GlcNac)3] was co-crystallized from 1.5% TEL and 2 mM (GlcNac)3 at pH, 4.2. The crystal structure was determined by molecular replacement and, refined to an R value of 0.182 using 10-1.77 A data. The (GlcNac)3, molecule occupies the subsites A, B and C. At the subsites B and C, the, sugar residues are bound in a similar manner to that found in the hen-egg, lysozyme (HEL) complex. In contrast, the GlcNac residue at the subsite A, is exposed to bulk solvent and has no contact with the protein molecule, because the active residue Asp101 in HEL is replaced by Gly in TEL. A, sulfate ion is bound in the vicinity of subsite B and forms hydrogen bonds, with the sugar residue and the guanidino group of Arg61, assisting the, binding of the sugar residue to subsite B. The active-site cleft of TEL is, narrower than that of native TEL, thus attaining the best fit of the, (GlcNac)3 molecule. The lack of binding ability of subsite A is discussed, in relation to the catalytic properties of TEL. The result suggests that, the cleavage pattern of oligosaccharide substrates in the catalytic, reaction is regulated by the protein-sugar interaction at subsite A.
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<StructureSection load='1jef' size='340' side='right'caption='[[1jef]], [[Resolution|resolution]] 1.77&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1jef]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Meleagris_gallopavo Meleagris gallopavo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JEF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JEF 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]] 1.77&#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=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PRD_900017:triacetyl-beta-chitotriose'>PRD_900017</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1jef FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jef OCA], [https://pdbe.org/1jef PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jef RCSB], [https://www.ebi.ac.uk/pdbsum/1jef PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jef ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/LYSC_MELGA LYSC_MELGA] 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.
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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/je/1jef_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1jef ConSurf].
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<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 turkey-egg lysozyme (TEL) complex with tri-N-acetylchitotriose [(GlcNac)3] was co-crystallized from 1.5% TEL and 2 mM (GlcNac)3 at pH 4.2. The crystal structure was determined by molecular replacement and refined to an R value of 0.182 using 10-1.77 A data. The (GlcNac)3 molecule occupies the subsites A, B and C. At the subsites B and C, the sugar residues are bound in a similar manner to that found in the hen-egg lysozyme (HEL) complex. In contrast, the GlcNac residue at the subsite A is exposed to bulk solvent and has no contact with the protein molecule because the active residue Asp101 in HEL is replaced by Gly in TEL. A sulfate ion is bound in the vicinity of subsite B and forms hydrogen bonds with the sugar residue and the guanidino group of Arg61, assisting the binding of the sugar residue to subsite B. The active-site cleft of TEL is narrower than that of native TEL, thus attaining the best fit of the (GlcNac)3 molecule. The lack of binding ability of subsite A is discussed in relation to the catalytic properties of TEL. The result suggests that the cleavage pattern of oligosaccharide substrates in the catalytic reaction is regulated by the protein-sugar interaction at subsite A.
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==About this Structure==
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X-ray structure of turkey-egg lysozyme complex with tri-N-acetylchitotriose. Lack of binding ability at subsite A.,Harata K, Muraki M Acta Crystallogr D Biol Crystallogr. 1997 Nov 1;53(Pt 6):650-7. PMID:15299852<ref>PMID:15299852</ref>
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1JEF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Meleagris_gallopavo Meleagris gallopavo] with SO4 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=1JEF OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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X-ray structure of turkey-egg lysozyme complex with tri-N-acetylchitotriose. Lack of binding ability at subsite A., Harata K, Muraki M, Acta Crystallogr D Biol Crystallogr. 1997 Nov 1;53(Pt 6):650-7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15299852 15299852]
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</div>
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[[Category: Lysozyme]]
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<div class="pdbe-citations 1jef" style="background-color:#fffaf0;"></div>
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[[Category: Meleagris gallopavo]]
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[[Category: Single protein]]
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[[Category: Harata, K.]]
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[[Category: Muraki, M.]]
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[[Category: SO4]]
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[[Category: bacteriolytic enzyme]]
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[[Category: enzyme]]
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[[Category: glycosidase]]
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[[Category: hydrolase]]
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[[Category: inhibitor complex]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:09:54 2007''
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==See Also==
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*[[Lysozyme 3D structures|Lysozyme 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Meleagris gallopavo]]
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[[Category: Harata K]]
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[[Category: Muraki M]]

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TURKEY LYSOZYME COMPLEX WITH (GLCNAC)3

PDB ID 1jef

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