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1lkr

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(New page: 200px<br /><applet load="1lkr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lkr, resolution 1.6&Aring;" /> '''MONOCLINIC HEN EGG WH...)
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[[Image:1lkr.jpg|left|200px]]<br /><applet load="1lkr" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1lkr, resolution 1.6&Aring;" />
 
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'''MONOCLINIC HEN EGG WHITE LYSOZYME IODIDE'''<br />
 
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==Overview==
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==MONOCLINIC HEN EGG WHITE LYSOZYME IODIDE==
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Hen egg-white lysozyme is one of the most thoroughly studied of enzymes, and has been the subject of study by many methods, including X-ray, crystallography. The present work extends the X-ray crystallography to, higher resolution, includes the positions of the anions, and examines the, contacts of the neighbors in greater detail. Data were collected at room, temperature on a Rigaku R-axis area detector with rotating-anode X-ray, generator to 1.6 A resolution for monoclinic lysozyme iodide at pH 4.0, to, 1.8 A for monoclinic lysozyme iodide at pH 8.0, and to 1.1 A resolution, for triclinic lysozyme nitrate at pH 4.5. The structures have been refined, by SHELX93 with the expected number of anion sites being accounted for., Two regions of the protein have been found to be variable: residues 65-75, and 99-104. Except for 65-75 and 99-104, lysozyme is a very stable, molecule with the crystal forms being held together by the electrostatic, contacts of the anions and by layers of water molecules. The anion, positions can be described as paired half sites, each half being, contributed by a different lysozyme molecule. The many different crystal, forms of lysozyme may be due to different combinations of the many such, half sites on the surface. A hypothesis is presented for lysozyme in the, different crystal forms and which may be extended to behavior in solution., Suggestions for future crystallographic research are proposed, involving, anions of different shape and charge.
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<StructureSection load='1lkr' size='340' side='right'caption='[[1lkr]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1lkr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LKR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LKR 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=IOD:IODIDE+ION'>IOD</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=1lkr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lkr OCA], [https://pdbe.org/1lkr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lkr RCSB], [https://www.ebi.ac.uk/pdbsum/1lkr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lkr ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/LYSC_CHICK LYSC_CHICK] 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. Has bacteriolytic activity against M.luteus.<ref>PMID:22044478</ref>
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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/lk/1lkr_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=1lkr 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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1LKR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with IOD 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LKR OCA].
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*[[Lysozyme 3D structures|Lysozyme 3D structures]]
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== References ==
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==Reference==
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<references/>
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Structures of monoclinic lysozyme iodide at 1.6 A and of triclinic lysozyme nitrate at 1.1 A., Steinrauf LK, Acta Crystallogr D Biol Crystallogr. 1998 Sep 1;54(Pt 5):767-80. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9757091 9757091]
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__TOC__
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</StructureSection>
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
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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: Steinrauf LK]]
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[[Category: Steinrauf, L.K.]]
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[[Category: IOD]]
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[[Category: glycosidase]]
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[[Category: hydrolase]]
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[[Category: lysozyme]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:38:02 2007''
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MONOCLINIC HEN EGG WHITE LYSOZYME IODIDE

PDB ID 1lkr

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