1jj0: Difference between revisions
No edit summary |
No edit summary |
||
| (7 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==CRYSTAL STRUCTURE OF TETRAGONAL LYSOZYME GROWN IN PRESENCE of 30% SUCROSE== | ==CRYSTAL STRUCTURE OF TETRAGONAL LYSOZYME GROWN IN PRESENCE of 30% SUCROSE== | ||
<StructureSection load='1jj0' size='340' side='right' caption='[[1jj0]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='1jj0' size='340' side='right'caption='[[1jj0]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1jj0]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1jj0]] 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=1JJ0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JJ0 FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> | ||
<tr><td class="sblockLbl"><b> | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FRU:FRUCTOSE'>FRU</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900003:sucrose'>PRD_900003</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1jj0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jj0 OCA], [https://pdbe.org/1jj0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jj0 RCSB], [https://www.ebi.ac.uk/pdbsum/1jj0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jj0 ProSAT]</span></td></tr> | ||
<table> | </table> | ||
== 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]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jj/1jj0_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jj/1jj0_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
</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/ | </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=1jj0 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
| Line 25: | Line 28: | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1jj0" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
| Line 33: | Line 37: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Gallus gallus]] | [[Category: Gallus gallus]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Biswal | [[Category: Biswal BK]] | ||
[[Category: Datta | [[Category: Datta S]] | ||
[[Category: Vijayan | [[Category: Vijayan M]] | ||
Latest revision as of 09:49, 30 October 2024
CRYSTAL STRUCTURE OF TETRAGONAL LYSOZYME GROWN IN PRESENCE of 30% SUCROSECRYSTAL STRUCTURE OF TETRAGONAL LYSOZYME GROWN IN PRESENCE of 30% SUCROSE
Structural highlights
FunctionLYSC_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.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedIn order to elucidate the effect of stabilizing additives on the structure of proteins and the associated ordered water molecules in the hydration shell, the crystal structures of tetragonal lysozyme grown in the presence of sucrose, sorbitol and trehalose have been refined. Also refined are the structures of orthorhombic and monoclinic lysozyme grown under the conditions in which tetragonal lysozyme is normally grown. A comparison of the two sets of structures with the structure of native tetragonal lysozyme shows that the effect of the additives on the structure of the protein molecule is less than that of the normal minor changes associated with differences in molecular packing. Surprisingly, the same is true of the effect on the hydration shell, represented by the ordered water molecules attached to the protein. Thus, it appears that the cause of the stabilizing effect of the additives needs to be sought outside the immediate neighbourhood of the protein molecule. Sorbitol and trehalose do not coherently interact with the protein. One sucrose molecule binds at the active-site cleft of the enzyme. The effect of stabilizing additives on the structure and hydration of proteins: a study involving tetragonal lysozyme.,Datta S, Biswal BK, Vijayan M Acta Crystallogr D Biol Crystallogr. 2001 Nov;57(Pt 11):1614-20. Epub 2001, Oct 25. PMID:11679726[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||