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1qsw

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(New page: 200px<br /> <applet load="1qsw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qsw, resolution 1.85&Aring;" /> '''CRYSTAL STRUCTURE A...)
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[[Image:1qsw.gif|left|200px]]<br />
 
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<applet load="1qsw" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1qsw, resolution 1.85&Aring;" />
 
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'''CRYSTAL STRUCTURE ANALYSIS OF A HUMAN LYSOZYME MUTANT W64C C65A'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE ANALYSIS OF A HUMAN LYSOZYME MUTANT W64C C65A==
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The three-dimensional structure of a mutant human lysozyme, W64CC65A, in, which a non-native disulfide bond Cys64--Cys81 is substituted for the, Cys65--Cys81 of the wild type protein by replacing Trp64 and Cys65 with, Cys and Ala, respectively, was determined by X-ray crystallography and, refined to an R-value of 0.181, using 33,187 reflections at 1.87-A, resolution. The refined model of the W64CC65A protein consisted of four, molecules, which were related by two noncrystallographic twofold axes and, a translation vector. Although no specific structural differences could be, observed among these four molecules, the overall B-factors of each, molecule were quite different. The overall structure of W64CC65A, especially in the alpha-helical domain, was found to be quite similar to, that of the wild type protein. Moreover, the side-chain conformation of, the newly formed Cys64--Cys81 bond was quite similar to that of the, Cys65--Cys81 bond of the wild-type protein. However, in the beta-sheet, domain, the main-chain atoms of the loop region from positions 66-75 could, not be determined, and significant structural changes due to the formation, of the non-native disulfide bond could be observed. From these results, it, is clear that the loop region of the mutant protein does not fold with the, specific folding as observed in the wild-type protein.
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<StructureSection load='1qsw' size='340' side='right'caption='[[1qsw]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1qsw]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QSW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QSW 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]] 1.85&#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=1qsw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qsw OCA], [https://pdbe.org/1qsw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qsw RCSB], [https://www.ebi.ac.uk/pdbsum/1qsw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qsw ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/LYSC_HUMAN LYSC_HUMAN] Defects in LYZ are a cause of amyloidosis type 8 (AMYL8) [MIM:[https://omim.org/entry/105200 105200]; also known as systemic non-neuropathic amyloidosis or Ostertag-type amyloidosis. AMYL8 is a hereditary generalized amyloidosis due to deposition of apolipoprotein A1, fibrinogen and lysozyme amyloids. Viscera are particularly affected. There is no involvement of the nervous system. Clinical features include renal amyloidosis resulting in nephrotic syndrome, arterial hypertension, hepatosplenomegaly, cholestasis, petechial skin rash.<ref>PMID:8464497</ref>
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== Function ==
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[https://www.uniprot.org/uniprot/LYSC_HUMAN LYSC_HUMAN] 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.
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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/qs/1qsw_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=1qsw ConSurf].
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<div style="clear:both"></div>
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==Disease==
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==See Also==
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Known diseases associated with this structure: Amyloidosis, renal OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=153450 153450]], Microphthalmia, syndromic 1 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=309800 309800]]
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*[[Lysozyme 3D structures|Lysozyme 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1QSW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QSW OCA].
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__TOC__
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</StructureSection>
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==Reference==
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Crystal structure of a mutant human lysozyme with a substituted disulfide bond., Inaka K, Kanaya E, Kikuchi M, Miki K, Proteins. 2001 Jun 1;43(4):413-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11340658 11340658]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Inaka, K.]]
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[[Category: Inaka K]]
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[[Category: Kanaya, E.]]
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[[Category: Kanaya E]]
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[[Category: Kikuchi, M.]]
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[[Category: Kikuchi M]]
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[[Category: Miki, K.]]
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[[Category: Miki K]]
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[[Category: hydrolase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:56:24 2007''
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Current revision

CRYSTAL STRUCTURE ANALYSIS OF A HUMAN LYSOZYME MUTANT W64C C65A

PDB ID 1qsw

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