1lj4
From Proteopedia
(Difference between revisions)
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<StructureSection load='1lj4' size='340' side='right'caption='[[1lj4]], [[Resolution|resolution]] 1.95Å' scene=''> | <StructureSection load='1lj4' size='340' side='right'caption='[[1lj4]], [[Resolution|resolution]] 1.95Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[1lj4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1lj4]] 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=1LJ4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LJ4 FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95Å</td></tr> |
- | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></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=1lj4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lj4 OCA], [https://pdbe.org/1lj4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lj4 RCSB], [https://www.ebi.ac.uk/pdbsum/1lj4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lj4 ProSAT]</span></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=1lj4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lj4 OCA], [https://pdbe.org/1lj4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lj4 RCSB], [https://www.ebi.ac.uk/pdbsum/1lj4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lj4 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
- | + | [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> | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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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=1lj4 ConSurf]. | </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=1lj4 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | In pursuance of a long-range programme on the hydration, mobility and action of proteins, the structural basis of the stabilizing effect of sugars and polyols is being investigated. With two crystallographically independent molecules with slightly different packing environments in the crystal, monoclinic lysozyme constitutes an ideal system for exploring the problem. The differences in the structure and hydration of the two molecules provide a framework for examining the changes caused by stabilizing additives. Monoclinic crystals were grown under native conditions and also in the presence of 10% sucrose, 15% trehalose, 10% trehalose, 10% sorbitol and 5% glycerol. The crystal structures were refined at resolutions ranging from 1.8 to 2.1 A. The average B values, and hence the mobility of the structure, are lower in the presence of additives than in the native crystals. However, a comparison of the structures indicates that the effect of the additives on the structure and the hydration shell around the protein molecule is considerably less than that caused by differences in packing. It is also less than that caused by the replacement of NaNO(3) by NaCl as the precipitant in the crystallization experiments. This result is not in conformity with the commonly held belief that additives exert their stabilizing effect through the reorganization of the hydration shell, at least as far as the ordered water molecules are concerned. | ||
- | |||
- | Effect of stabilizing additives on the structure and hydration of proteins: a study involving monoclinic lysozyme.,Saraswathi NT, Sankaranarayanan R, Vijayan M Acta Crystallogr D Biol Crystallogr. 2002 Jul;58(Pt 7):1162-7. Epub 2002, Jun 20. PMID:12077436<ref>PMID:12077436</ref> | ||
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- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 1lj4" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: | + | [[Category: Gallus gallus]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | + | [[Category: Sankaranarayanan R]] | |
- | [[Category: Sankaranarayanan | + | [[Category: Saraswathi NT]] |
- | [[Category: Saraswathi | + | [[Category: Vijayan M]] |
- | [[Category: Vijayan | + | |
- | + | ||
- | + |
Revision as of 08:09, 3 April 2024
CRYSTAL STRUCTURE OF MONOCLINIC LYSOZYME GROWN AT PH 4.6
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