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New page: left|200px<br /><applet load="135l" size="450" color="white" frame="true" align="right" spinBox="true" caption="135l, resolution 1.30Å" /> '''X-RAY STRUCTURE OF M...
 
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[[Image:135l.gif|left|200px]]<br /><applet load="135l" size="450" color="white" frame="true" align="right" spinBox="true"
caption="135l, resolution 1.30&Aring;" />
'''X-RAY STRUCTURE OF MONOCLINIC TURKEY EGG LYSOZYME AT 1.3 ANGSTROMS RESOLUTION'''<br />


==Overview==
==X-RAY STRUCTURE OF MONOCLINIC TURKEY EGG LYSOZYME AT 1.3 ANGSTROMS RESOLUTION==
Monoclinic crystals of turkey egg lysozyme (TEL, E.C. 3.2.1.17) were, obtained from 2.2 M ammonium sulfate solution at pH 4.2. They belong to, space group P2(1) with unit-cell dimensions a = 38.07, b = 33.20, c =, 46.12 A and beta = 110.1 degrees, and contain one molecule in the, asymmetric unit (V(m) = 1.91 A(3) Da(-1)). The three-dimensional structure, of TEL was solved by the method of multiple isomorphous replacement with, anomalous scattering. Area detector data to 1.5 A resolution from native, and heavy-atom derivatives were used for the structure determination. The, structure was refined by the simulated-annealing method with diffraction, data of 10-1.30 A resolution. The conventional R factor was 0.189. The, root-mean-square deviations from ideal bond distances and angles were, 0.016 A and 2.9 degrees, respectively. The backbone structure of TEL is, very similar to that of hen egg lysozyme (HEL) and the difference in seven, amino-acid residues does not affect the basic folding of the polypeptide, chain. Except for the region from Gly101 to Gly104, the geometry of the, active-site cleft is conserved between TEL and HEL. The Gly101 residue is, located at the end of the sugar-binding site and the structural change in, this region between TEL and HEL is considered to be responsible for the, difference in their enzymatic properties.
<StructureSection load='135l' size='340' side='right'caption='[[135l]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[135l]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Meleagris_gallopavo Meleagris gallopavo]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1lz3 1lz3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=135L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=135L FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.3&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=135l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=135l OCA], [https://pdbe.org/135l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=135l RCSB], [https://www.ebi.ac.uk/pdbsum/135l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=135l ProSAT]</span></td></tr>
</table>
== Function ==
[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.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/35/135l_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=135l ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
135L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. This structure superseeds the now removed PDB entry 1LZ3. 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=135L OCA].
*[[Lysozyme 3D structures|Lysozyme 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
X-ray structure of monoclinic turkey egg lysozyme at 1.3 A resolution., Harata K, Acta Crystallogr D Biol Crystallogr. 1993 Sep 1;49(Pt 5):497-504. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15299509 15299509]
[[Category: Large Structures]]
[[Category: Lysozyme]]
[[Category: Meleagris gallopavo]]
[[Category: Single protein]]
[[Category: Harata K]]
[[Category: Harata, K.]]
[[Category: hydrolase(o-glycosyl)]]
 
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