2z2e: Difference between revisions
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==Crystal Structure of Canine Milk Lysozyme Stabilized against Non-enzymatic Deamidation== | |||
<StructureSection load='2z2e' size='340' side='right'caption='[[2z2e]], [[Resolution|resolution]] 2.01Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2z2e]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Canis_lupus_familiaris Canis lupus familiaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Z2E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Z2E FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.01Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=2z2e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2z2e OCA], [https://pdbe.org/2z2e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2z2e RCSB], [https://www.ebi.ac.uk/pdbsum/2z2e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2z2e ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/LYSC1_CANLF LYSC1_CANLF] 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.[PROSITE-ProRule:PRU00680] | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/z2/2z2e_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</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/main_output.php?pdb_ID=2z2e ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Asparaginyl deamidation is a common form of nonenzymatic degradation of proteins and peptides. As it introduces a negative charge spontaneously and irreversibly, charge heterogeneity can be accumulated in protein solution during purification, preservation, and experiments. In this study, canine milk lysozyme (CML), a useful model for the study of the molten globule state, exhibited charge heterogeneity after sample purification. Four Asn residues in CML deamidated rapidly under mild conditions: pH 8.0 and 30 degrees C. Other than these residues, one Asn residue, which was stable in the native state, was labile to deamidation in the unfolded state. This suggests that the structural formation around Asn can suppress deamidation. Substitutions of these labile Asn residues to Gln residues prevented deamidation effectively. Because the substitutions did not disrupt the structural formation of the native and molten globule states, they will enable more precise analyses for physical and structural studies. Proteins 2008. (c) 2008 Wiley-Liss, Inc. | |||
Spontaneous asparaginyl deamidation of canine milk lysozyme under mild conditions.,Nonaka Y, Aizawa T, Akieda D, Yasui M, Watanabe M, Watanabe N, Tanaka I, Kamiya M, Mizuguchi M, Demura M, Kawano K Proteins. 2008 Jan 23;72(1):313-322. PMID:18214981<ref>PMID:18214981</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2z2e" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
*[[Lysozyme 3D structures|Lysozyme 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Canis lupus familiaris]] | [[Category: Canis lupus familiaris]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Aizawa T]] | |||
[[Category: Aizawa | [[Category: Akieda D]] | ||
[[Category: Akieda | [[Category: Demura M]] | ||
[[Category: Demura | [[Category: Kamiya M]] | ||
[[Category: Kamiya | [[Category: Kawano K]] | ||
[[Category: Kawano | [[Category: Nitta K]] | ||
[[Category: Nitta | [[Category: Nonaka Y]] | ||
[[Category: Nonaka | [[Category: Tanaka I]] | ||
[[Category: Tanaka | [[Category: Watanabe N]] | ||
[[Category: Watanabe | |||
Latest revision as of 09:39, 6 November 2024
Crystal Structure of Canine Milk Lysozyme Stabilized against Non-enzymatic Deamidation
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