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132l

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(New page: 200px<br /><applet load="132l" size="450" color="white" frame="true" align="right" spinBox="true" caption="132l, resolution 1.8&Aring;" /> '''STRUCTURAL CONSEQUENC...)
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[[Image:132l.gif|left|200px]]<br /><applet load="132l" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="132l, resolution 1.8&Aring;" />
 
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'''STRUCTURAL CONSEQUENCES OF REDUCTIVE METHYLATION OF LYSINE RESIDUES IN HEN EGG WHITE LYSOZYME: AN X-RAY ANALYSIS AT 1.8 ANGSTROMS RESOLUTION'''<br />
 
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==Overview==
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==STRUCTURAL CONSEQUENCES OF REDUCTIVE METHYLATION OF LYSINE RESIDUES IN HEN EGG WHITE LYSOZYME: AN X-RAY ANALYSIS AT 1.8 ANGSTROMS RESOLUTION==
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Chemical modification of proteins has been and continues to be an, important biochemical tool for the study of protein structure and, function. One such type of approach has been the reductive methylation of, lysine residues. In order to address the consequences of such methylation, on the crystallization and structural properties of a protein, the, three-dimensional structure of hen egg white lysozyme in which all lysine, residues have been alkylated has been determined and refined to a nominal, resolution of 1.8 A and a crystallographic R factor of 17.3%. Crystals, used in the investigation were grown from 1.5-1.8 M MgSO4 and 50 mM Tris, at pH 8.0 and belonged to the space group P2(1)2(1)2(1) with unit cell, dimensions of a = 30.6 A, b = 56.3 A, c = 73.2 A, and one molecule per, asymmetric unit. It was not possible to grow crystals of the modified, lysozyme under the conditions normally employed for the hen egg white, protein. Overall, the three-dimensional structures of the native lysozyme, and the modified protein are very similar with only two surface loops, differing to any significant extent. Specifically, the positions of the, alpha-carbons for these two forms of the protein, excluding the surface, loops, superimpose with a root-mean-square value of 0.40 A. The magnitude, of the structural changes observed between the modified an unmodified, forms of lysozyme is similar to that seen when an identical protein, structure is solved in two different crystalline lattices.(ABSTRACT, TRUNCATED AT 250 WORDS)
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<StructureSection load='132l' size='340' side='right'caption='[[132l]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[132l]] 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=132L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=132L 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]] 1.8&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DM0:N~2~,N~2~,N~6~,N~6~-TETRAMETHYL-L-LYSINE'>DM0</scene>, <scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene></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=132l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=132l OCA], [https://pdbe.org/132l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=132l RCSB], [https://www.ebi.ac.uk/pdbsum/132l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=132l 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/32/132l_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=132l ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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132L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with DML as [http://en.wikipedia.org/wiki/ligand ligand]. 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=132L OCA].
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*[[Lysozyme 3D structures|Lysozyme 3D structures]]
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== References ==
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==Reference==
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<references/>
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Structural consequences of reductive methylation of lysine residues in hen egg white lysozyme: an X-ray analysis at 1.8-A resolution., Rypniewski WR, Holden HM, Rayment I, Biochemistry. 1993 Sep 21;32(37):9851-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8373783 8373783]
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__TOC__
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[[Category: Lysozyme]]
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</StructureSection>
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[[Category: Single protein]]
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[[Category: Gallus gallus]]
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[[Category: Holden, H.M.]]
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[[Category: Large Structures]]
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[[Category: Rayment, I.]]
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[[Category: Holden HM]]
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[[Category: Rypniewski, W.R.]]
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[[Category: Rayment I]]
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[[Category: DML]]
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[[Category: Rypniewski WR]]
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[[Category: hydrolase(o-glycosyl)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:26:38 2007''
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Current revision

STRUCTURAL CONSEQUENCES OF REDUCTIVE METHYLATION OF LYSINE RESIDUES IN HEN EGG WHITE LYSOZYME: AN X-RAY ANALYSIS AT 1.8 ANGSTROMS RESOLUTION

PDB ID 132l

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