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133l

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[[Image:133l.gif|left|200px]]
 
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==ROLE OF ARG 115 IN THE CATALYTIC ACTION OF HUMAN LYSOZYME. X-RAY STRUCTURE OF HIS 115 AND GLU 115 MUTANTS==
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The line below this paragraph, containing "STRUCTURE_133l", creates the "Structure Box" on the page.
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<StructureSection load='133l' size='340' side='right'caption='[[133l]], [[Resolution|resolution]] 1.77&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[133l]] is a 1 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=133L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=133L FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 1.77&#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=133l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=133l OCA], [https://pdbe.org/133l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=133l RCSB], [https://www.ebi.ac.uk/pdbsum/133l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=133l ProSAT]</span></td></tr>
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{{STRUCTURE_133l| PDB=133l | SCENE= }}
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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/33/133l_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=133l ConSurf].
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<div style="clear:both"></div>
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'''ROLE OF ARG 115 IN THE CATALYTIC ACTION OF HUMAN LYSOZYME. X-RAY STRUCTURE OF HIS 115 AND GLU 115 MUTANTS'''
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==See Also==
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*[[Lysozyme 3D structures|Lysozyme 3D structures]]
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== References ==
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==Overview==
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<references/>
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The structure of modified human lysozymes (HLs), in which Arg115 is replaced by His or Glu, has been investigated by X-ray analysis at 1.77 A resolution. The mutation of the 115th residue by His does not affect the backbone structure as indicated by a root-mean-square deviation (r.m.s.d) of 0.14 A for the superposition of equivalent C alpha atoms between His115 HL and wild-type HL. In contrast, the corresponding r.m.s.d. value for Glu115 HL is 0.38 A which is twice as large as the estimated co-ordinate error of 0.2 A. Movement of the backbone structure is observed in the region of residues 100 to 130, which give an r.m.s.d. value of 0.61 A and a maximum deviation of 1.46 A for Arg119. A significant movement is also observed in the region of residues 45 to 50, which are located at the opposite side of the region of residues 100 to 120 with respect to the active site cleft. As a result, the active site cleft of Glu115 HL is narrower than the cleft of His115 HL or wild-type HL. This structural change is considered to be responsible for the low catalytic activity of Glu115 HL and the change of the catalytic property found in the hydrolysis of oligosaccharides. The replacement of Arg115 by Glu changes the charge distribution in the molecule, and the change in the electrostatic field may affect polar interactions among residues. The side-chain group of His115 and Glu115 is almost parallel to the indole moiety of Trp34, but the carboxyl group of Glu115 is laterally shifted to avoid overlapping with the indole moiety. The carboxylate anion of Glu115, which does not favor the face-to-face contact with aromatic groups, may provide a driving force for the structural change. The prominent structural change caused by the single mutation suggests that Arg115 is a key residue in maintaining the structure of the active site cleft.
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__TOC__
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</StructureSection>
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==About this Structure==
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133L is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=133L OCA].
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==Reference==
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Role of Arg115 in the catalytic action of human lysozyme. X-ray structure of His115 and Glu115 mutants., Harata K, Muraki M, Jigami Y, J Mol Biol. 1993 Oct 5;233(3):524-35. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8105095 8105095]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Lysozyme]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Harata K]]
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[[Category: Harata, K.]]
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[[Category: Jigami Y]]
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[[Category: Jigami, Y.]]
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[[Category: Muraki M]]
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[[Category: Muraki, M.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 09:29:01 2008''
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Current revision

ROLE OF ARG 115 IN THE CATALYTIC ACTION OF HUMAN LYSOZYME. X-RAY STRUCTURE OF HIS 115 AND GLU 115 MUTANTS

PDB ID 133l

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