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154l

From Proteopedia

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[[Image:154l.gif|left|200px]]
 
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{{Structure
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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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|PDB= 154l |SIZE=350|CAPTION= <scene name='initialview01'>154l</scene>, resolution 1.6&Aring;
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<StructureSection load='154l' size='340' side='right'caption='[[154l]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>
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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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|ACTIVITY= <span class='plainlinks'>[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] </span>
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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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|GENE=
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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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|DOMAIN=
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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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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=154l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=154l OCA], [http://www.ebi.ac.uk/pdbsum/154l PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=154l RCSB]</span>
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== Function ==
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}}
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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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'''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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==See Also==
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*[[Lysozyme 3D structures|Lysozyme 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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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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[[Category: Anser anser anser]]
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[[Category: Large Structures]]
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==About this Structure==
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[[Category: Gruetter MG]]
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154L is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=154L OCA].
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[[Category: Matthews BW]]
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[[Category: Weaver LH]]
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==Reference==
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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://www.ncbi.nlm.nih.gov/pubmed/7823320 7823320]
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[[Category: Lysozyme]]
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[[Category: Single protein]]
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[[Category: Gruetter, M G.]]
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[[Category: Matthews, B W.]]
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[[Category: Weaver, L H.]]
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[[Category: hydrolase(o-glycosyl)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:28:25 2008''
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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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