4lym

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(New page: 200px<br /><applet load="4lym" size="450" color="white" frame="true" align="right" spinBox="true" caption="4lym, resolution 2.1&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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[[Image:4lym.jpg|left|200px]]<br /><applet load="4lym" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="4lym, resolution 2.1&Aring;" />
 
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'''CRYSTAL STRUCTURE OF LOW HUMIDITY TETRAGONAL LYSOZYME AT 2.1-ANGSTROMS RESOLUTION. VARIABILITY IN HYDRATION SHELL AND ITS STRUCTURAL CONSEQUENCES'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF LOW HUMIDITY TETRAGONAL LYSOZYME AT 2.1-ANGSTROMS RESOLUTION. VARIABILITY IN HYDRATION SHELL AND ITS STRUCTURAL CONSEQUENCES==
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Tetragonal crystals of hen egg white lysozyme undergo a reversible, transformation, accompanied by loss of water, when the relative humidity, of the environment is reduced to about 90%. The structure of the low, humidity form has been analyzed, using x-ray data collected at 88%, relative humidity, in order to explore the variability in protein, hydration caused by a change in the amount of water surrounding the, protein molecule and the consequent conformational perturbations in the, molecule. The structure has been refined by the restrained least-squares, method to an R value of 0.162 for 6269 observed reflections in the, 10-2.1-A resolution shell. The refined structure provides interesting, examples for the variability in helical parameters, the role of, interactions involving side chains and water in the stabilization of, secondary structural features, and favorable specific hydration sites. The, protein molecule as a whole moves slightly in the low humidity form from, its position in the native crystals. The hydration shell tends to move, along with the protein. Significant changes, however, occur in the, hydration shell. These changes cause structural perturbations in the, enzyme molecule, which are most pronounced in regions involved in, substrate binding.
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<StructureSection load='4lym' size='340' side='right'caption='[[4lym]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4lym]] is a 1 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=4LYM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LYM 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]] 2.1&#8491;</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=4lym FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lym OCA], [https://pdbe.org/4lym PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lym RCSB], [https://www.ebi.ac.uk/pdbsum/4lym PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lym 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/ly/4lym_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=4lym 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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Tetragonal crystals of hen egg white lysozyme undergo a reversible transformation, accompanied by loss of water, when the relative humidity of the environment is reduced to about 90%. The structure of the low humidity form has been analyzed, using x-ray data collected at 88% relative humidity, in order to explore the variability in protein hydration caused by a change in the amount of water surrounding the protein molecule and the consequent conformational perturbations in the molecule. The structure has been refined by the restrained least-squares method to an R value of 0.162 for 6269 observed reflections in the 10-2.1-A resolution shell. The refined structure provides interesting examples for the variability in helical parameters, the role of interactions involving side chains and water in the stabilization of secondary structural features, and favorable specific hydration sites. The protein molecule as a whole moves slightly in the low humidity form from its position in the native crystals. The hydration shell tends to move along with the protein. Significant changes, however, occur in the hydration shell. These changes cause structural perturbations in the enzyme molecule, which are most pronounced in regions involved in substrate binding.
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==About this Structure==
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Crystal structure of low humidity tetragonal lysozyme at 2.1-A resolution. Variability in hydration shell and its structural consequences.,Kodandapani R, Suresh CG, Vijayan M J Biol Chem. 1990 Sep 25;265(27):16126-31. PMID:2398048<ref>PMID:2398048</ref>
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4LYM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. 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=4LYM 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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Crystal structure of low humidity tetragonal lysozyme at 2.1-A resolution. Variability in hydration shell and its structural consequences., Kodandapani R, Suresh CG, Vijayan M, J Biol Chem. 1990 Sep 25;265(27):16126-31. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=2398048 2398048]
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</div>
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[[Category: Gallus gallus]]
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<div class="pdbe-citations 4lym" style="background-color:#fffaf0;"></div>
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[[Category: Lysozyme]]
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[[Category: Single protein]]
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[[Category: Kodandapani, R.]]
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[[Category: Suresh, C.G.]]
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[[Category: Vijayan, M.]]
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[[Category: hydrolase (o-glycosyl)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:40:38 2007''
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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: Gallus gallus]]
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[[Category: Large Structures]]
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[[Category: Kodandapani R]]
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[[Category: Suresh CG]]
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[[Category: Vijayan M]]

Current revision

CRYSTAL STRUCTURE OF LOW HUMIDITY TETRAGONAL LYSOZYME AT 2.1-ANGSTROMS RESOLUTION. VARIABILITY IN HYDRATION SHELL AND ITS STRUCTURAL CONSEQUENCES

PDB ID 4lym

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