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1uco

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(New page: 200px<br /><applet load="1uco" size="450" color="white" frame="true" align="right" spinBox="true" caption="1uco, resolution 2.0&Aring;" /> '''HEN EGG-WHITE LYSOZYM...)
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[[Image:1uco.jpg|left|200px]]<br /><applet load="1uco" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1uco, resolution 2.0&Aring;" />
 
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'''HEN EGG-WHITE LYSOZYME, LOW HUMIDITY FORM'''<br />
 
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==Overview==
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==HEN EGG-WHITE LYSOZYME, LOW HUMIDITY FORM==
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The atomic models of native monoclinic lysozyme obtained by refinement at, Bangalore and elsewhere [Young, Dewan, Nave &amp; Tilton (1993). J. Appl., Cryst. 26, 309-319] differed significantly in the flexible regions of the, protein molecule. The two models were reconciled starting from regions, where they were in reasonable agreement to produce an improved model which, yielded an R value of 0.169 for 12 816 observed reflections in the 10-2 A, resolution range. The reconciled model was compared with the structure of, the 88% relative humidity form obtained through a water-mediated, transformation [Madhusudan, Kodandapani &amp; Vijayan (1993). Acta Cryst. D49, 234-245]. Parts of the flexible regions of the molecule register, significant movements during the transformation. The changes resulting, from the transformation from the native to the low-humidity forms are, pronounced in many of the side chains in the active-site region, thus, indicating the relationship between hydration, mobility and enzyme action., The fact that the overall changes in molecular geometry resulting from, water-mediated transformation are similar to those which occur during, enzyme action, further emphasizes this relationship.
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<StructureSection load='1uco' size='340' side='right'caption='[[1uco]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1uco]] 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=1UCO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UCO 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&#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=1uco FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uco OCA], [https://pdbe.org/1uco PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uco RCSB], [https://www.ebi.ac.uk/pdbsum/1uco PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uco 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/uc/1uco_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=1uco 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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The atomic models of native monoclinic lysozyme obtained by refinement at Bangalore and elsewhere [Young, Dewan, Nave &amp; Tilton (1993). J. Appl. Cryst. 26, 309-319] differed significantly in the flexible regions of the protein molecule. The two models were reconciled starting from regions where they were in reasonable agreement to produce an improved model which yielded an R value of 0.169 for 12 816 observed reflections in the 10-2 A resolution range. The reconciled model was compared with the structure of the 88% relative humidity form obtained through a water-mediated transformation [Madhusudan, Kodandapani &amp; Vijayan (1993). Acta Cryst. D49, 234-245]. Parts of the flexible regions of the molecule register significant movements during the transformation. The changes resulting from the transformation from the native to the low-humidity forms are pronounced in many of the side chains in the active-site region, thus indicating the relationship between hydration, mobility and enzyme action. The fact that the overall changes in molecular geometry resulting from water-mediated transformation are similar to those which occur during enzyme action, further emphasizes this relationship.
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==About this Structure==
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An X-ray analysis of native monoclinic lysozyme. A case study on the reliability of refined protein structures and a comparison with the low-humidity form in relation to mobility and enzyme action.,Nagendra HG, Sudarsanakumar C, Vijayan M Acta Crystallogr D Biol Crystallogr. 1996 Nov 1;52(Pt 6):1067-74. PMID:15299565<ref>PMID:15299565</ref>
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1UCO 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=1UCO 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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An X-ray analysis of native monoclinic lysozyme. A case study on the reliability of refined protein structures and a comparison with the low-humidity form in relation to mobility and enzyme action., Nagendra HG, Sudarsanakumar C, Vijayan M, Acta Crystallogr D Biol Crystallogr. 1996 Nov 1;52(Pt 6):1067-74. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15299565 15299565]
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</div>
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[[Category: Gallus gallus]]
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<div class="pdbe-citations 1uco" style="background-color:#fffaf0;"></div>
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[[Category: Lysozyme]]
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[[Category: Single protein]]
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[[Category: Nagendra, H.G.]]
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[[Category: Sudarsanakumar, C.]]
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[[Category: Vijayan, M.]]
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[[Category: enzyme-monoclinic form]]
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[[Category: hydrolase]]
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[[Category: o-glycosyl]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 04:01:19 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: Nagendra HG]]
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[[Category: Sudarsanakumar C]]
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[[Category: Vijayan M]]

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HEN EGG-WHITE LYSOZYME, LOW HUMIDITY FORM

PDB ID 1uco

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