3lz2

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[[Image:3lz2.jpg|left|200px]]
 
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{{Structure
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==STRUCTURE DETERMINATION OF TURKEY EGG WHITE LYSOZYME USING LAUE DIFFRACTION==
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|PDB= 3lz2 |SIZE=350|CAPTION= <scene name='initialview01'>3lz2</scene>, resolution 2.5&Aring;
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<StructureSection load='3lz2' size='340' side='right'caption='[[3lz2]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[3lz2]] 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=3LZ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LZ2 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]] 2.5&#8491;</td></tr>
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|GENE=
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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=3lz2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lz2 OCA], [https://pdbe.org/3lz2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lz2 RCSB], [https://www.ebi.ac.uk/pdbsum/3lz2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lz2 ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3lz2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lz2 OCA], [http://www.ebi.ac.uk/pdbsum/3lz2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3lz2 RCSB]</span>
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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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}}
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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/lz/3lz2_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=3lz2 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 three-dimensional structure of turkey egg-white lysozyme (TEWL) has been solved and refined at 2.5 A resolution using X-ray data collected by the Laue method. This is the first protein structure determination undertaken using Laue diffraction data. A re-examination of the existing structure of TEWL was necessary when attempts to refine an atomic model based on the C alpha positions in the Protein Data Bank (entry 1LZ2) failed. The correct orientation and position of the turkey lysozyme molecules within the crystallographic unit cell were determined by molecular replacement using a refined model of the homologous hen egg-white lysozyme crystal structure. After modification of the model to reflect the differences in amino-acid sequence between the chicken and turkey enzymes, the structure was subjected to crystallographic refinement using the simulated-annealing refinement technique and conventional least-squares refinement. This yielded a final residual of R = 20.7%. This crystal form is of potential interest for time-resolved crystallographic studies since the amino-acid residues involved in catalysis (Asp52 and Glu35) are accessible to solvent and not blocked by crystal contacts.
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'''STRUCTURE DETERMINATION OF TURKEY EGG WHITE LYSOZYME USING LAUE DIFFRACTION'''
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Structure determination of turkey egg-white lysozyme using Laue diffraction data.,Howell PL, Almo SC, Parsons MR, Hajdu J, Petsko GA Acta Crystallogr B. 1992 Apr 1;48 ( Pt 2):200-7. PMID:1515108<ref>PMID:1515108</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3lz2" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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The three-dimensional structure of turkey egg-white lysozyme (TEWL) has been solved and refined at 2.5 A resolution using X-ray data collected by the Laue method. This is the first protein structure determination undertaken using Laue diffraction data. A re-examination of the existing structure of TEWL was necessary when attempts to refine an atomic model based on the C alpha positions in the Protein Data Bank (entry 1LZ2) failed. The correct orientation and position of the turkey lysozyme molecules within the crystallographic unit cell were determined by molecular replacement using a refined model of the homologous hen egg-white lysozyme crystal structure. After modification of the model to reflect the differences in amino-acid sequence between the chicken and turkey enzymes, the structure was subjected to crystallographic refinement using the simulated-annealing refinement technique and conventional least-squares refinement. This yielded a final residual of R = 20.7%. This crystal form is of potential interest for time-resolved crystallographic studies since the amino-acid residues involved in catalysis (Asp52 and Glu35) are accessible to solvent and not blocked by crystal contacts.
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*[[Lysozyme 3D structures|Lysozyme 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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3LZ2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Meleagris_gallopavo Meleagris gallopavo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LZ2 OCA].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Large Structures]]
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Structure determination of turkey egg-white lysozyme using Laue diffraction data., Howell PL, Almo SC, Parsons MR, Hajdu J, Petsko GA, Acta Crystallogr B. 1992 Apr 1;48 ( Pt 2):200-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1515108 1515108]
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[[Category: Lysozyme]]
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[[Category: Meleagris gallopavo]]
[[Category: Meleagris gallopavo]]
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[[Category: Single protein]]
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[[Category: Almo SC]]
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[[Category: Almo, S C.]]
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[[Category: Hajdu J]]
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[[Category: Hajdu, J.]]
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[[Category: Howell PL]]
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[[Category: Howell, P L.]]
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[[Category: Parsons MR]]
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[[Category: Parsons, M R.]]
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[[Category: Petsko GA]]
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[[Category: Petsko, G A.]]
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[[Category: hydrolase(o-glycosyl)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:34:35 2008''
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Current revision

STRUCTURE DETERMINATION OF TURKEY EGG WHITE LYSOZYME USING LAUE DIFFRACTION

PDB ID 3lz2

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