1tew

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[[Image:1tew.jpg|left|200px]]<br /><applet load="1tew" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1tew, resolution 1.65&Aring;" />
 
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'''STRUCTURE OF HEXAGONAL TURKEY EGG WHITE LYSOZYME AT 1.65 ANGSTROMS RESOLUTION'''<br />
 
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==Overview==
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==STRUCTURE OF HEXAGONAL TURKEY EGG WHITE LYSOZYME AT 1.65 ANGSTROMS RESOLUTION==
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<StructureSection load='1tew' size='340' side='right'caption='[[1tew]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1tew]] 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=1TEW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TEW 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]] 1.65&#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=SCN:THIOCYANATE+ION'>SCN</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=1tew FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tew OCA], [https://pdbe.org/1tew PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tew RCSB], [https://www.ebi.ac.uk/pdbsum/1tew PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tew 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/te/1tew_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=1tew 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 ==
The structure of hexagonal turkey egg-white lysozyme (TEWL) has been determined and refined at 1.65 A resolution. The crystals were grown from a 150 mM potassium thiocyanate solution at pH 4.5 and belong to space group P6(1)22 with unit-cell dimensions a = b = 70.96, c = 83.01 A alpha = beta = 90, gamma = 120 degrees. The crystals were isomorphous with those of hexagonal pH 8.0 TEWL. The coordinates of PDB entry code 3LZ2 were therefore used as the initial model and subjected to rigid-body refinement, simulated annealing and least-squares refinement to a final residual of 0.20. The root-mean-square deviations from the ideal bond distances and angles were 0.016 A and 2.2 degrees, respectively. During the refinement, 86 water molecules and one thiocyanate ion were located in the structure. The thiocyanate ion lies close to the interface between two symmetry-related molecules. The S atom of the ion forms two direct intermolecular contacts with Argl4 and interacts indirectly via a network of water molecules to Arg5 of a symmetry-related molecule. The structure provides direct evidence for the mode of thiocyanate binding to arginine residues and suggests a possible mechanism for the efficiency of thiocyanate in crystallizing basic proteins.
The structure of hexagonal turkey egg-white lysozyme (TEWL) has been determined and refined at 1.65 A resolution. The crystals were grown from a 150 mM potassium thiocyanate solution at pH 4.5 and belong to space group P6(1)22 with unit-cell dimensions a = b = 70.96, c = 83.01 A alpha = beta = 90, gamma = 120 degrees. The crystals were isomorphous with those of hexagonal pH 8.0 TEWL. The coordinates of PDB entry code 3LZ2 were therefore used as the initial model and subjected to rigid-body refinement, simulated annealing and least-squares refinement to a final residual of 0.20. The root-mean-square deviations from the ideal bond distances and angles were 0.016 A and 2.2 degrees, respectively. During the refinement, 86 water molecules and one thiocyanate ion were located in the structure. The thiocyanate ion lies close to the interface between two symmetry-related molecules. The S atom of the ion forms two direct intermolecular contacts with Argl4 and interacts indirectly via a network of water molecules to Arg5 of a symmetry-related molecule. The structure provides direct evidence for the mode of thiocyanate binding to arginine residues and suggests a possible mechanism for the efficiency of thiocyanate in crystallizing basic proteins.
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==About this Structure==
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Structure of hexagonal turkey egg-white lysozyme at 1.65A resolution.,Howell PL Acta Crystallogr D Biol Crystallogr. 1995 Sep 1;51(Pt 5):654-62. PMID:15299795<ref>PMID:15299795</ref>
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1TEW 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 <scene name='pdbligand=SCN:'>SCN</scene> 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1TEW 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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Structure of hexagonal turkey egg-white lysozyme at 1.65A resolution., Howell PL, Acta Crystallogr D Biol Crystallogr. 1995 Sep 1;51(Pt 5):654-62. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15299795 15299795]
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</div>
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[[Category: Lysozyme]]
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<div class="pdbe-citations 1tew" style="background-color:#fffaf0;"></div>
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[[Category: Meleagris gallopavo]]
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[[Category: Single protein]]
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[[Category: Howell, P L.]]
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[[Category: SCN]]
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[[Category: hydrolase(o-glycosyl)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:12:50 2008''
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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: Howell PL]]

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STRUCTURE OF HEXAGONAL TURKEY EGG WHITE LYSOZYME AT 1.65 ANGSTROMS RESOLUTION

PDB ID 1tew

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