1xei

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[[Image:1xei.gif|left|200px]]<br /><applet load="1xei" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1xei, resolution 2.1&Aring;" />
 
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'''THE CRYSTAL STRUCTURES OF LYSOZYME AT VERY LOW LEVELS OF HYDRATION'''<br />
 
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==Overview==
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==THE CRYSTAL STRUCTURES OF LYSOZYME AT VERY LOW LEVELS OF HYDRATION==
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Earlier studies involving water-mediated transformations in lysozyme and, ribonuclease A have shown that the overall movements in the protein, molecule consequent to the reduction in the amount of surrounding water, are similar to those that occur during enzyme action, thus highlighting, the relationship among hydration, plasticity, and action of these enzymes., Monoclinic lysozyme retains its crystallinity even when the level of, hydration is reduced further below that necessary for activity (about 0.2, gram of water per gram of protein). In order to gain insights into the, role of water in the stability and the plasticity of the protein molecule, and the geometrical basis for the loss of activity that accompanies, dehydration, the crystal structures of monoclinic lysozyme with solvent, contents of 17.6%, 16.9%, and 9.4% were determined and refined. A detailed, comparison of these forms with the normally hydrated forms show that the, C-terminal segment (residues 88-129) of domain I and the main loop, (residues 65-73) in domain II exhibit large deviations in atomic positions, when the solvent content is reduced, although the three-dimensional, structure is essentially preserved. Many crucial water bridges between, different regions of the molecule are conserved in spite of differences in, detail, even when the level of hydration is reduced well below that, required for activity. The loss of activity that accompany dehydration, appears to be caused by the removal of functionally important water, molecules from the active-site region and the reduction in the size of the, substrate binding cleft.
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<StructureSection load='1xei' size='340' side='right'caption='[[1xei]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1xei]] 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=1XEI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XEI 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=1xei FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xei OCA], [https://pdbe.org/1xei PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xei RCSB], [https://www.ebi.ac.uk/pdbsum/1xei PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xei 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/xe/1xei_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=1xei 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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1XEI 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] Known structural/functional Site: <scene name='pdbsite=CAT:Active+Site'>CAT</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XEI 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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Role of water in plasticity, stability, and action of proteins: the crystal structures of lysozyme at very low levels of hydration., Nagendra HG, Sukumar N, Vijayan M, Proteins. 1998 Aug 1;32(2):229-40. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9714162 9714162]
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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: Nagendra HG]]
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[[Category: Nagendra, H.G.]]
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[[Category: Sukumar N]]
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[[Category: Sukumar, N.]]
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[[Category: Vijayan M]]
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[[Category: Vijayan, M.]]
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[[Category: enzyme monoclinic 38% r.h. form i]]
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[[Category: hydrolase]]
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[[Category: o-glycosyl]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:21:57 2008''
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Current revision

THE CRYSTAL STRUCTURES OF LYSOZYME AT VERY LOW LEVELS OF HYDRATION

PDB ID 1xei

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