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154l

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(New page: 200px<br /><applet load="154l" size="450" color="white" frame="true" align="right" spinBox="true" caption="154l, resolution 1.6&Aring;" /> '''THE REFINED STRUCTURE...)
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[[Image:154l.gif|left|200px]]<br /><applet load="154l" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="154l, resolution 1.6&Aring;" />
 
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'''THE REFINED STRUCTURES OF GOOSE LYSOZYME AND ITS COMPLEX WITH A BOUND TRISACCHARIDE SHOW THAT THE "GOOSE-TYPE LYSOZYMES LACK A CATALYTIC ASPARTATE'''<br />
 
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==Overview==
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==THE REFINED STRUCTURES OF GOOSE LYSOZYME AND ITS COMPLEX WITH A BOUND TRISACCHARIDE SHOW THAT THE "GOOSE-TYPE LYSOZYMES LACK A CATALYTIC ASPARTATE==
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The structure of goose egg-white lysozyme (GEWL) has been refined to an, R-value of 15.9% at 1.6 A resolution. Details of the structure, determination, the refinement and the structure itself are presented. The, structure of a complex of the enzyme with the trisaccharide of N-acetyl, glucosamine has also been determined and refined at 1.6 A resolution. The, trisaccharide occupies sites analogous to the B, C and D subsites of, chicken (HEWL) and phage T4 (T4L) lysozymes. All three lysozymes (GEWL, HEWL and T4L) display the same characteristic set of bridging hydrogen, bonds between backbone atoms of the protein and the 2-acetamido group of, the saccharide in subsite C. Glu73 of GEWL is seen to correspond closely, to Glu35 of HEWL (and to Glu11 of T4L) and supports the established view, that this group is critically involved in the catalytic mechanism. There, is, however, no obvious residue in goose lysozyme that is a counterpart of, Asp52 of chicken lysozyme (or of Asp20 in T4L), suggesting that a second, acidic residue is not essential for the catalytic activity of goose, lysozyme, and may not be required for the activity of other lysozymes.
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<StructureSection load='154l' size='340' side='right'caption='[[154l]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[154l]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Anser_anser_anser Anser anser anser]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=154L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=154L 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]] 1.6&#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></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=154l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=154l OCA], [https://pdbe.org/154l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=154l RCSB], [https://www.ebi.ac.uk/pdbsum/154l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=154l ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/LYG_ANSAN LYG_ANSAN]
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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/54/154l_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=154l 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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154L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. 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=154L OCA].
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*[[Lysozyme 3D structures|Lysozyme 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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The refined structures of goose lysozyme and its complex with a bound trisaccharide show that the "goose-type" lysozymes lack a catalytic aspartate residue., Weaver LH, Grutter MG, Matthews BW, J Mol Biol. 1995 Jan 6;245(1):54-68. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7823320 7823320]
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[[Category: Anser anser anser]]
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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: Gruetter MG]]
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[[Category: Gruetter, M.G.]]
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[[Category: Matthews BW]]
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[[Category: Matthews, B.W.]]
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[[Category: Weaver LH]]
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[[Category: Weaver, L.H.]]
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[[Category: hydrolase(o-glycosyl)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:28:01 2007''
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Current revision

THE REFINED STRUCTURES OF GOOSE LYSOZYME AND ITS COMPLEX WITH A BOUND TRISACCHARIDE SHOW THAT THE "GOOSE-TYPE LYSOZYMES LACK A CATALYTIC ASPARTATE

PDB ID 154l

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