134l - Revision history

OCA at 15:19, 13 March 2024

OCA — Wed, 13 Mar 2024 15:19:52 GMT

←Older revision		Revision as of 15:19, 13 March 2024
Line 3:		Line 3:
	<StructureSection load='134l' size='340' side='right'caption='[[134l]], [[Resolution\|resolution]] 1.77Å' scene=''>		<StructureSection load='134l' size='340' side='right'caption='[[134l]], [[Resolution\|resolution]] 1.77Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[134l]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=134L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=134L FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[134l]] 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=134L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=134L FirstGlance]. <br>
-	</td></tr><tr id='~~activity~~'><td class="sblockLbl"><b>~~Activity~~:</b></td><td class="sblockDat"~~><span class~~=~~'plainlinks'~~>[~~https://en.wikipedia.org/wiki/Lysozyme Lysozyme~~]~~, with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.~~1.~~17 3.2.1.17] </span>~~</td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 1.77Å</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=134l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=134l OCA], [https://pdbe.org/134l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=134l RCSB], [https://www.ebi.ac.uk/pdbsum/134l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=134l ProSAT]</span></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=134l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=134l OCA], [https://pdbe.org/134l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=134l RCSB], [https://www.ebi.ac.uk/pdbsum/134l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=134l ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[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>	+	[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>
	== Function ==		== Function ==
-	[[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.	+	[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.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 21:		Line 21:
	</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=134l ConSurf].		</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=134l ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	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.
-
-	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:8105095<ref>PMID:8105095</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 134l" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 37:		Line 28:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Lysozyme]]~~	+	[[Category: Harata K]]
-	[[Category: Harata, K]]	+	[[Category: Jigami Y]]
-	[[Category: Jigami, Y]]	+	[[Category: Muraki M]]
-	[[Category: Muraki, M]]	+

OCA at 10:24, 14 July 2021

OCA — Wed, 14 Jul 2021 10:24:35 GMT

←Older revision		Revision as of 10:24, 14 July 2021
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	<StructureSection load='134l' size='340' side='right'caption='[[134l]], [[Resolution\|resolution]] 1.77Å' scene=''>		<StructureSection load='134l' size='340' side='right'caption='[[134l]], [[Resolution\|resolution]] 1.77Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[134l]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=134L OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=134L FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[134l]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=134L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=134L FirstGlance]. <br>
-	</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~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] </span></td></tr>	+	</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=134l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=134l OCA], [~~http~~://pdbe.org/134l PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=134l RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/134l PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=134l ProSAT]</span></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=134l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=134l OCA], [https://pdbe.org/134l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=134l RCSB], [https://www.ebi.ac.uk/pdbsum/134l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=134l ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/LYSC_HUMAN LYSC_HUMAN]] Defects in LYZ are a cause of amyloidosis type 8 (AMYL8) [MIM:[~~http~~://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>	+	[[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>
	== Function ==		== Function ==
-	[[~~http~~://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.	+	[[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.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 07:17, 10 October 2019

OCA — Thu, 10 Oct 2019 07:17:17 GMT

←Older revision		Revision as of 07:17, 10 October 2019
Line 1:		Line 1:

	==ROLE OF ARG 115 IN THE CATALYTIC ACTION OF HUMAN LYSOZYME. X-RAY STRUCTURE OF HIS 115 AND GLU 115 MUTANTS==		==ROLE OF ARG 115 IN THE CATALYTIC ACTION OF HUMAN LYSOZYME. X-RAY STRUCTURE OF HIS 115 AND GLU 115 MUTANTS==
-	<StructureSection load='134l' size='340' side='right' caption='[[134l]], [[Resolution\|resolution]] 1.77Å' scene=''>	+	<StructureSection load='134l' size='340' side='right'caption='[[134l]], [[Resolution\|resolution]] 1.77Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[134l]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=134L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=134L FirstGlance]. <br>		<table><tr><td colspan='2'>[[134l]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=134L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=134L FirstGlance]. <br>
Line 15:		Line 15:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/34/134l_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/34/134l_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
Line 38:		Line 38:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Lysozyme]]		[[Category: Lysozyme]]
	[[Category: Harata, K]]		[[Category: Harata, K]]
	[[Category: Jigami, Y]]		[[Category: Jigami, Y]]
	[[Category: Muraki, M]]		[[Category: Muraki, M]]

OCA at 10:42, 15 November 2017

OCA — Wed, 15 Nov 2017 10:42:36 GMT

←Older revision		Revision as of 10:42, 15 November 2017
Line 1:		Line 1:
		+
	==ROLE OF ARG 115 IN THE CATALYTIC ACTION OF HUMAN LYSOZYME. X-RAY STRUCTURE OF HIS 115 AND GLU 115 MUTANTS==		==ROLE OF ARG 115 IN THE CATALYTIC ACTION OF HUMAN LYSOZYME. X-RAY STRUCTURE OF HIS 115 AND GLU 115 MUTANTS==
	<StructureSection load='134l' size='340' side='right' caption='[[134l]], [[Resolution\|resolution]] 1.77Å' scene=''>		<StructureSection load='134l' size='340' side='right' caption='[[134l]], [[Resolution\|resolution]] 1.77Å' scene=''>
Line 4:		Line 5:
	<table><tr><td colspan='2'>[[134l]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=134L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=134L FirstGlance]. <br>		<table><tr><td colspan='2'>[[134l]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=134L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=134L FirstGlance]. <br>
	</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>		</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=134l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=134l OCA], [http://pdbe.org/134l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=134l RCSB], [http://www.ebi.ac.uk/pdbsum/134l PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=134l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=134l OCA], [http://pdbe.org/134l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=134l RCSB], [http://www.ebi.ac.uk/pdbsum/134l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=134l ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==

OCA at 12:00, 8 February 2016

OCA — Mon, 08 Feb 2016 12:00:35 GMT

←Older revision		Revision as of 12:00, 8 February 2016
Line 18:		Line 18:
	<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/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</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=134l ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 15:55, 9 September 2015

OCA — Wed, 09 Sep 2015 15:55:40 GMT

←Older revision		Revision as of 15:55, 9 September 2015
Line 2:		Line 2:
	<StructureSection load='134l' size='340' side='right' caption='[[134l]], [[Resolution\|resolution]] 1.77Å' scene=''>		<StructureSection load='134l' size='340' side='right' caption='[[134l]], [[Resolution\|resolution]] 1.77Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[134l]] is a 1 chain structure with 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=134L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=134L FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[134l]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=134L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=134L FirstGlance]. <br>
	</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>		</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=134l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=134l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=134l RCSB], [http://www.ebi.ac.uk/pdbsum/134l PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=134l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=134l OCA], [http://pdbe.org/134l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=134l RCSB], [http://www.ebi.ac.uk/pdbsum/134l PDBsum]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 28:		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 134l" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 35:		Line 36:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Lysozyme]]		[[Category: Lysozyme]]
	[[Category: Harata, K]]		[[Category: Harata, K]]
	[[Category: Jigami, Y]]		[[Category: Jigami, Y]]
	[[Category: Muraki, M]]		[[Category: Muraki, M]]

OCA at 10:11, 22 December 2014

OCA — Mon, 22 Dec 2014 10:11:24 GMT

←Older revision		Revision as of 10:11, 22 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[134l]] is a 1 chain structure with 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=134L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=134L FirstGlance]. <br>		<table><tr><td colspan='2'>[[134l]] is a 1 chain structure with 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=134L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=134L FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>	+	</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=134l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=134l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=134l RCSB], [http://www.ebi.ac.uk/pdbsum/134l PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=134l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=134l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=134l RCSB], [http://www.ebi.ac.uk/pdbsum/134l PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Disease ==		== Disease ==
	[[http://www.uniprot.org/uniprot/LYSC_HUMAN LYSC_HUMAN]] Defects in LYZ are a cause of amyloidosis type 8 (AMYL8) [MIM:[http://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>		[[http://www.uniprot.org/uniprot/LYSC_HUMAN LYSC_HUMAN]] Defects in LYZ are a cause of amyloidosis type 8 (AMYL8) [MIM:[http://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>
Line 37:		Line 37:
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Lysozyme]]		[[Category: Lysozyme]]
-	[[Category: Harata, K.]]	+	[[Category: Harata, K]]
-	[[Category: Jigami, Y.]]	+	[[Category: Jigami, Y]]
-	[[Category: Muraki, M.]]	+	[[Category: Muraki, M]]

OCA at 14:44, 29 September 2014

OCA — Mon, 29 Sep 2014 14:44:45 GMT

←Older revision		Revision as of 14:44, 29 September 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_134l\| PDB=134l \| SCENE= }}~~	+	==ROLE OF ARG 115 IN THE CATALYTIC ACTION OF HUMAN LYSOZYME. X-RAY STRUCTURE OF HIS 115 AND GLU 115 MUTANTS==
-	===ROLE OF ARG 115 IN THE CATALYTIC ACTION OF HUMAN LYSOZYME. X-RAY STRUCTURE OF HIS 115 AND GLU 115 MUTANTS===	+	<StructureSection load='134l' size='340' side='right' caption='[[134l]], [[Resolution\|resolution]] 1.77Å' scene=''>
-	~~{{ABSTRACT_PUBMED_8105095}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[134l]] is a 1 chain structure with 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=134L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=134L FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=134l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=134l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=134l RCSB], [http://www.ebi.ac.uk/pdbsum/134l PDBsum]</span></td></tr>
		+	<table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/LYSC_HUMAN LYSC_HUMAN]] Defects in LYZ are a cause of amyloidosis type 8 (AMYL8) [MIM:[http://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>
		+	== Function ==
		+	[[http://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.
		+	== 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/34/134l_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	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.

-	~~==Disease==~~	+	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:8105095<ref>PMID:8105095</ref>
-	~~[[http://www.uniprot.org/uniprot/LYSC_HUMAN LYSC_HUMAN]] Defects~~ in ~~LYZ are a cause~~ of ~~amyloidosis type 8 (AMYL8) [MIM:[http://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>	+

-	~~==Function==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[http:~~/~~/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~~.	+	</div>
-		+
-	~~==About this Structure==~~	+
-	~~[[134l]] is a 1 chain structure with 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=134L OCA].~~	+

	==See Also==		==See Also==
-	*[[~~Hen Egg-White (HEW)~~ Lysozyme\|~~Hen Egg-White (HEW)~~ Lysozyme]]	+	*[[Lysozyme 3D structures\|Lysozyme 3D structures]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:008105095</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Lysozyme]]		[[Category: Lysozyme]]

OCA at 11:38, 24 March 2013

OCA — Sun, 24 Mar 2013 11:38:34 GMT

←Older revision		Revision as of 11:38, 24 March 2013
Line 1:		Line 1:
-	[[Image:134l.png\|left\|200px]]
-
	{{STRUCTURE_134l\| PDB=134l \| SCENE= }}		{{STRUCTURE_134l\| PDB=134l \| SCENE= }}
-
	===ROLE OF ARG 115 IN THE CATALYTIC ACTION OF HUMAN LYSOZYME. X-RAY STRUCTURE OF HIS 115 AND GLU 115 MUTANTS===		===ROLE OF ARG 115 IN THE CATALYTIC ACTION OF HUMAN LYSOZYME. X-RAY STRUCTURE OF HIS 115 AND GLU 115 MUTANTS===
		+	{{ABSTRACT_PUBMED_8105095}}

-	~~{{ABSTRACT_PUBMED_8105095}}~~	+	==Disease==
		+	[[http://www.uniprot.org/uniprot/LYSC_HUMAN LYSC_HUMAN]] Defects in LYZ are a cause of amyloidosis type 8 (AMYL8) [MIM:[http://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>
		+
		+	==Function==
		+	[[http://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.

	==About this Structure==		==About this Structure==
Line 14:		Line 16:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:008105095</ref><references group="xtra"/>	+	<ref group="xtra">PMID:008105095</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Lysozyme]]		[[Category: Lysozyme]]

OCA at 10:03, 20 October 2012

OCA — Sat, 20 Oct 2012 10:03:47 GMT

←Older revision		Revision as of 10:03, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[134l]] is a 1 chain structure ~~of [[Hen Egg-White (HEW) Lysozyme]]~~ with 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=134L OCA].	+	[[134l]] is a 1 chain structure with 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=134L OCA].

	==See Also==		==See Also==