1cu3 - Revision history

OCA at 06:45, 7 February 2024

OCA — Wed, 07 Feb 2024 06:45:49 GMT

←Older revision		Revision as of 06:45, 7 February 2024
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	<StructureSection load='1cu3' size='340' side='right'caption='[[1cu3]], [[Resolution\|resolution]] 2.12Å' scene=''>		<StructureSection load='1cu3' size='340' side='right'caption='[[1cu3]], [[Resolution\|resolution]] 2.12Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1cu3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Bpt4 Bpt4~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CU3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CU3 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1cu3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CU3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CU3 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>~~, ~~<scene name='pdbligand=HED:~~2~~-HYDROXYETHYL+DISULFIDE'>HED</scene>~~</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]] 2.12Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max-height: 3em;~~'>[[1ctw\|1ctw]], [[1cu0\|1cu0]], [[1cu2\|1cu2]], [[1cu6\|1cu6]], [[1cu5\|1cu5]], [[1cup\|1cup]], [[1cuq\|1cuq]], [[1cv0\|1cv0]], [[1cv1\|1cv1]], [[1qsq\|1qsq]], [[1cv4\|1cv4]], [[1cv3\|1cv3]], [[1cv5\|1cv5]], [[1cv6\|1cv6]], [[1cvk\|1cvk]], [[1d2w\|1d2w]], [[1d2y\|1d2y]], [[1d3f\|1d3f]], [[1d3j\|1d3j]]</~~div~~><~~/td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=HED:2-HYDROXYETHYL+DISULFIDE'>HED</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=1cu3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cu3 OCA], [https://pdbe.org/1cu3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cu3 RCSB], [https://www.ebi.ac.uk/pdbsum/1cu3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cu3 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=1cu3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cu3 OCA], [https://pdbe.org/1cu3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cu3 RCSB], [https://www.ebi.ac.uk/pdbsum/1cu3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cu3 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/~~LYS_BPT4 LYS_BPT4~~]~~] Helps~~ to ~~release~~ the mature ~~phage~~ particles ~~from~~ the cell ~~wall by breaking~~ down the peptidoglycan.	+	[https://www.uniprot.org/uniprot/ENLYS_BPT4 ENLYS_BPT4] Endolysin with lysozyme activity that degrades host peptidoglycans and participates with the holin and spanin proteins in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles. Once the holin has permeabilized the host cell membrane, the endolysin can reach the periplasm and break down the peptidoglycan layer.<ref>PMID:22389108</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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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=1cu3 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=1cu3 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	In an attempt to identify a systematic relation between the structure of a protein and its folding kinetics, the rate of folding was determined for 20 mutants of T4 lysozyme in which a bulky, buried, nonpolar wild-type residue (Leu, Ile, Phe, Val, or Met) was substituted with alanine. Methionine, which approximated the size of the original side chain but which is of different shape and flexibility, was also substituted at most of the same sites. Mutations that substantially destabilize the protein and are located in the carboxy-terminal domain generally slow the rate of folding. Destabilizing mutations in the amino-terminal domain, however, have little effect on the rate of folding. Mutations that have little effect on stability tend to have little effect on the rate, no matter where they are located. These results suggest that, at the rate-limiting step, elements of structure in the C-terminal domain are formed and have a structure similar to that of the fully folded protein. Consistent with this, two variants that somewhat increase the rate of folding (Phe104 --> Met and Val149 --> Met) are located within the carboxy-terminal domain and maintain or improve packing with very little perturbation of the wild-type structure.
-
-	Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding.,Gassner NC, Baase WA, Lindstrom JD, Lu J, Dahlquist FW, Matthews BW Biochemistry. 1999 Nov 2;38(44):14451-60. PMID:10545167<ref>PMID:10545167</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1cu3" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Bpt4~~]]	+	[[Category: Escherichia virus T4]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Lysozyme]]~~	+	[[Category: Baase WA]]
-	[[Category: Baase~~, W A~~]]	+	[[Category: Gassner NC]]
-	[[Category: Gassner~~, N C~~]]	+	[[Category: Lindstrom JD]]
-	[[Category: Lindstrom~~, J D~~]]	+	[[Category: Lu J]]
-	[[Category: Lu, J]]	+	[[Category: Matthews BW]]
-	[[Category: Matthews~~, B W]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Methionine core mutant]]~~	+
-	~~[[Category: Protein engineering]]~~	+
-	~~[[Category: Protein folding]]~~	+
-	~~[[Category: T4 lysozyme~~]]	+

OCA at 10:40, 14 July 2021

OCA — Wed, 14 Jul 2021 10:40:14 GMT

←Older revision		Revision as of 10:40, 14 July 2021
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	<StructureSection load='1cu3' size='340' side='right'caption='[[1cu3]], [[Resolution\|resolution]] 2.12Å' scene=''>		<StructureSection load='1cu3' size='340' side='right'caption='[[1cu3]], [[Resolution\|resolution]] 2.12Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1cu3]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Bpt4 Bpt4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CU3 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1CU3 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1cu3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bpt4 Bpt4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CU3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CU3 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=HED:2-HYDROXYETHYL+DISULFIDE'>HED</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=HED:2-HYDROXYETHYL+DISULFIDE'>HED</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ctw\|1ctw]], [[1cu0\|1cu0]], [[1cu2\|1cu2]], [[1cu6\|1cu6]], [[1cu5\|1cu5]], [[1cup\|1cup]], [[1cuq\|1cuq]], [[1cv0\|1cv0]], [[1cv1\|1cv1]], [[1qsq\|1qsq]], [[1cv4\|1cv4]], [[1cv3\|1cv3]], [[1cv5\|1cv5]], [[1cv6\|1cv6]], [[1cvk\|1cvk]], [[1d2w\|1d2w]], [[1d2y\|1d2y]], [[1d3f\|1d3f]], [[1d3j\|1d3j]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ctw\|1ctw]], [[1cu0\|1cu0]], [[1cu2\|1cu2]], [[1cu6\|1cu6]], [[1cu5\|1cu5]], [[1cup\|1cup]], [[1cuq\|1cuq]], [[1cv0\|1cv0]], [[1cv1\|1cv1]], [[1qsq\|1qsq]], [[1cv4\|1cv4]], [[1cv3\|1cv3]], [[1cv5\|1cv5]], [[1cv6\|1cv6]], [[1cvk\|1cvk]], [[1d2w\|1d2w]], [[1d2y\|1d2y]], [[1d3f\|1d3f]], [[1d3j\|1d3j]]</div></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='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=1cu3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cu3 OCA], [~~http~~://pdbe.org/1cu3 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1cu3 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1cu3 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1cu3 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=1cu3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cu3 OCA], [https://pdbe.org/1cu3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cu3 RCSB], [https://www.ebi.ac.uk/pdbsum/1cu3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cu3 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/LYS_BPT4 LYS_BPT4]] Helps to release the mature phage particles from the cell wall by breaking down the peptidoglycan.	+	[[https://www.uniprot.org/uniprot/LYS_BPT4 LYS_BPT4]] Helps to release the mature phage particles from the cell wall by breaking down the peptidoglycan.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 06:35, 10 October 2019

OCA — Thu, 10 Oct 2019 06:35:37 GMT

←Older revision		Revision as of 06:35, 10 October 2019
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	==T4 LYSOZYME MUTANT V87M==		==T4 LYSOZYME MUTANT V87M==
-	<StructureSection load='1cu3' size='340' side='right' caption='[[1cu3]], [[Resolution\|resolution]] 2.12Å' scene=''>	+	<StructureSection load='1cu3' size='340' side='right'caption='[[1cu3]], [[Resolution\|resolution]] 2.12Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1cu3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpt4 Bpt4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CU3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CU3 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1cu3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpt4 Bpt4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CU3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CU3 FirstGlance]. <br>
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	</StructureSection>		</StructureSection>
	[[Category: Bpt4]]		[[Category: Bpt4]]
		+	[[Category: Large Structures]]
	[[Category: Lysozyme]]		[[Category: Lysozyme]]
	[[Category: Baase, W A]]		[[Category: Baase, W A]]

OCA at 08:17, 6 December 2017

OCA — Wed, 06 Dec 2017 08:17:56 GMT

←Older revision		Revision as of 08:17, 6 December 2017
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		+
	==T4 LYSOZYME MUTANT V87M==		==T4 LYSOZYME MUTANT V87M==
	<StructureSection load='1cu3' size='340' side='right' caption='[[1cu3]], [[Resolution\|resolution]] 2.12Å' scene=''>		<StructureSection load='1cu3' size='340' side='right' caption='[[1cu3]], [[Resolution\|resolution]] 2.12Å' scene=''>
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	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ctw\|1ctw]], [[1cu0\|1cu0]], [[1cu2\|1cu2]], [[1cu6\|1cu6]], [[1cu5\|1cu5]], [[1cup\|1cup]], [[1cuq\|1cuq]], [[1cv0\|1cv0]], [[1cv1\|1cv1]], [[1qsq\|1qsq]], [[1cv4\|1cv4]], [[1cv3\|1cv3]], [[1cv5\|1cv5]], [[1cv6\|1cv6]], [[1cvk\|1cvk]], [[1d2w\|1d2w]], [[1d2y\|1d2y]], [[1d3f\|1d3f]], [[1d3j\|1d3j]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ctw\|1ctw]], [[1cu0\|1cu0]], [[1cu2\|1cu2]], [[1cu6\|1cu6]], [[1cu5\|1cu5]], [[1cup\|1cup]], [[1cuq\|1cuq]], [[1cv0\|1cv0]], [[1cv1\|1cv1]], [[1qsq\|1qsq]], [[1cv4\|1cv4]], [[1cv3\|1cv3]], [[1cv5\|1cv5]], [[1cv6\|1cv6]], [[1cvk\|1cvk]], [[1d2w\|1d2w]], [[1d2y\|1d2y]], [[1d3f\|1d3f]], [[1d3j\|1d3j]]</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='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=1cu3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cu3 OCA], [http://pdbe.org/1cu3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1cu3 RCSB], [http://www.ebi.ac.uk/pdbsum/1cu3 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=1cu3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cu3 OCA], [http://pdbe.org/1cu3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1cu3 RCSB], [http://www.ebi.ac.uk/pdbsum/1cu3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1cu3 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 14:		Line 15:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cu/1cu3_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cu/1cu3_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>

OCA at 07:08, 9 February 2016

OCA — Tue, 09 Feb 2016 07:08:09 GMT

←Older revision		Revision as of 07:08, 9 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=1cu3 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 19:49, 10 September 2015

OCA — Thu, 10 Sep 2015 19:49:07 GMT

←Older revision		Revision as of 19:49, 10 September 2015
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	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ctw\|1ctw]], [[1cu0\|1cu0]], [[1cu2\|1cu2]], [[1cu6\|1cu6]], [[1cu5\|1cu5]], [[1cup\|1cup]], [[1cuq\|1cuq]], [[1cv0\|1cv0]], [[1cv1\|1cv1]], [[1qsq\|1qsq]], [[1cv4\|1cv4]], [[1cv3\|1cv3]], [[1cv5\|1cv5]], [[1cv6\|1cv6]], [[1cvk\|1cvk]], [[1d2w\|1d2w]], [[1d2y\|1d2y]], [[1d3f\|1d3f]], [[1d3j\|1d3j]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ctw\|1ctw]], [[1cu0\|1cu0]], [[1cu2\|1cu2]], [[1cu6\|1cu6]], [[1cu5\|1cu5]], [[1cup\|1cup]], [[1cuq\|1cuq]], [[1cv0\|1cv0]], [[1cv1\|1cv1]], [[1qsq\|1qsq]], [[1cv4\|1cv4]], [[1cv3\|1cv3]], [[1cv5\|1cv5]], [[1cv6\|1cv6]], [[1cvk\|1cvk]], [[1d2w\|1d2w]], [[1d2y\|1d2y]], [[1d3f\|1d3f]], [[1d3j\|1d3j]]</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='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=1cu3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cu3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1cu3 RCSB], [http://www.ebi.ac.uk/pdbsum/1cu3 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=1cu3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cu3 OCA], [http://pdbe.org/1cu3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1cu3 RCSB], [http://www.ebi.ac.uk/pdbsum/1cu3 PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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 1cu3" style="background-color:#fffaf0;"></div>

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

OCA at 05:14, 25 December 2014

OCA — Thu, 25 Dec 2014 05:14:56 GMT

←Older revision		Revision as of 05:14, 25 December 2014
Line 8:		Line 8:
	<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=1cu3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cu3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1cu3 RCSB], [http://www.ebi.ac.uk/pdbsum/1cu3 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=1cu3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cu3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1cu3 RCSB], [http://www.ebi.ac.uk/pdbsum/1cu3 PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/LYS_BPT4 LYS_BPT4]] Helps to release the mature phage particles from the cell wall by breaking down the peptidoglycan.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 22:33, 22 December 2014

OCA — Mon, 22 Dec 2014 22:33:33 GMT

←Older revision		Revision as of 22:33, 22 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1cu3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpt4 Bpt4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CU3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CU3 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1cu3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpt4 Bpt4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CU3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CU3 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=HED:2-HYDROXYETHYL+DISULFIDE'>HED</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=HED:2-HYDROXYETHYL+DISULFIDE'>HED</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ctw\|1ctw]], [[1cu0\|1cu0]], [[1cu2\|1cu2]], [[1cu6\|1cu6]], [[1cu5\|1cu5]], [[1cup\|1cup]], [[1cuq\|1cuq]], [[1cv0\|1cv0]], [[1cv1\|1cv1]], [[1qsq\|1qsq]], [[1cv4\|1cv4]], [[1cv3\|1cv3]], [[1cv5\|1cv5]], [[1cv6\|1cv6]], [[1cvk\|1cvk]], [[1d2w\|1d2w]], [[1d2y\|1d2y]], [[1d3f\|1d3f]], [[1d3j\|1d3j]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ctw\|1ctw]], [[1cu0\|1cu0]], [[1cu2\|1cu2]], [[1cu6\|1cu6]], [[1cu5\|1cu5]], [[1cup\|1cup]], [[1cuq\|1cuq]], [[1cv0\|1cv0]], [[1cv1\|1cv1]], [[1qsq\|1qsq]], [[1cv4\|1cv4]], [[1cv3\|1cv3]], [[1cv5\|1cv5]], [[1cv6\|1cv6]], [[1cvk\|1cvk]], [[1d2w\|1d2w]], [[1d2y\|1d2y]], [[1d3f\|1d3f]], [[1d3j\|1d3j]]</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 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=1cu3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cu3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1cu3 RCSB], [http://www.ebi.ac.uk/pdbsum/1cu3 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=1cu3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cu3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1cu3 RCSB], [http://www.ebi.ac.uk/pdbsum/1cu3 PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 35:		Line 35:
	[[Category: Bpt4]]		[[Category: Bpt4]]
	[[Category: Lysozyme]]		[[Category: Lysozyme]]
-	[[Category: Baase, W A.]]	+	[[Category: Baase, W A]]
-	[[Category: Gassner, N C.]]	+	[[Category: Gassner, N C]]
-	[[Category: Lindstrom, J D.]]	+	[[Category: Lindstrom, J D]]
-	[[Category: Lu, J.]]	+	[[Category: Lu, J]]
-	[[Category: Matthews, B W.]]	+	[[Category: Matthews, B W]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
	[[Category: Methionine core mutant]]		[[Category: Methionine core mutant]]

OCA at 10:36, 3 October 2014

OCA — Fri, 03 Oct 2014 10:36:08 GMT

←Older revision		Revision as of 10:36, 3 October 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_1cu3~~\| ~~PDB~~=1cu3 \| ~~SCENE~~= }}	+	==T4 LYSOZYME MUTANT V87M==
-	===~~T4 LYSOZYME MUTANT V87M~~===	+	<StructureSection load='1cu3' size='340' side='right' caption='[[1cu3]], [[Resolution\|resolution]] 2.12Å' scene=''>
-	~~{{ABSTRACT_PUBMED_10545167}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1cu3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpt4 Bpt4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CU3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CU3 FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=HED:2-HYDROXYETHYL+DISULFIDE'>HED</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ctw\|1ctw]], [[1cu0\|1cu0]], [[1cu2\|1cu2]], [[1cu6\|1cu6]], [[1cu5\|1cu5]], [[1cup\|1cup]], [[1cuq\|1cuq]], [[1cv0\|1cv0]], [[1cv1\|1cv1]], [[1qsq\|1qsq]], [[1cv4\|1cv4]], [[1cv3\|1cv3]], [[1cv5\|1cv5]], [[1cv6\|1cv6]], [[1cvk\|1cvk]], [[1d2w\|1d2w]], [[1d2y\|1d2y]], [[1d3f\|1d3f]], [[1d3j\|1d3j]]</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=1cu3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cu3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1cu3 RCSB], [http://www.ebi.ac.uk/pdbsum/1cu3 PDBsum]</span></td></tr>
		+	<table>
		+	== 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/cu/1cu3_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 ==
		+	In an attempt to identify a systematic relation between the structure of a protein and its folding kinetics, the rate of folding was determined for 20 mutants of T4 lysozyme in which a bulky, buried, nonpolar wild-type residue (Leu, Ile, Phe, Val, or Met) was substituted with alanine. Methionine, which approximated the size of the original side chain but which is of different shape and flexibility, was also substituted at most of the same sites. Mutations that substantially destabilize the protein and are located in the carboxy-terminal domain generally slow the rate of folding. Destabilizing mutations in the amino-terminal domain, however, have little effect on the rate of folding. Mutations that have little effect on stability tend to have little effect on the rate, no matter where they are located. These results suggest that, at the rate-limiting step, elements of structure in the C-terminal domain are formed and have a structure similar to that of the fully folded protein. Consistent with this, two variants that somewhat increase the rate of folding (Phe104 --> Met and Val149 --> Met) are located within the carboxy-terminal domain and maintain or improve packing with very little perturbation of the wild-type structure.

-	~~==Function==~~	+	Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding.,Gassner NC, Baase WA, Lindstrom JD, Lu J, Dahlquist FW, Matthews BW Biochemistry. 1999 Nov 2;38(44):14451-60. PMID:10545167<ref>PMID:10545167</ref>
-	~~[[http~~:~~//www~~.~~uniprot.org~~/~~uniprot/LYS_BPT4 LYS_BPT4]] Helps to release the mature phage particles from the cell wall by breaking down the peptidoglycan.~~	+

-	~~==About this Structure==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[1cu3]] is~~ a ~~1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Bpt4 Bpt4]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1CU3 OCA].~~	+	</div>

	==See Also==		==See Also==
	*[[Lysozyme 3D structures\|Lysozyme 3D structures]]		*[[Lysozyme 3D structures\|Lysozyme 3D structures]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:010545167</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Bpt4]]		[[Category: Bpt4]]
	[[Category: Lysozyme]]		[[Category: Lysozyme]]

OCA at 07:15, 16 April 2014

OCA — Wed, 16 Apr 2014 07:15:50 GMT

←Older revision		Revision as of 07:15, 16 April 2014
Line 1:		Line 1:
-	[[Image:1cu3.png\|left\|200px]]
-
	{{STRUCTURE_1cu3\| PDB=1cu3 \| SCENE= }}		{{STRUCTURE_1cu3\| PDB=1cu3 \| SCENE= }}
-
	===T4 LYSOZYME MUTANT V87M===		===T4 LYSOZYME MUTANT V87M===
		+	{{ABSTRACT_PUBMED_10545167}}

-	~~{{ABSTRACT_PUBMED_10545167}}~~	+	==Function==
		+	[[http://www.uniprot.org/uniprot/LYS_BPT4 LYS_BPT4]] Helps to release the mature phage particles from the cell wall by breaking down the peptidoglycan.

	==About this Structure==		==About this Structure==
-	[[1cu3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Enterobacteria_phage_t4 Enterobacteria phage t4~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CU3 OCA].	+	[[1cu3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpt4 Bpt4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CU3 OCA].

	==See Also==		==See Also==
-	*[[~~Hen Egg-White (HEW)~~ Lysozyme\|~~Hen Egg-White (HEW)~~ Lysozyme]]	+	*[[Lysozyme 3D structures\|Lysozyme 3D structures]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:010545167</ref><references group="xtra"/>	+	<ref group="xtra">PMID:010545167</ref><references group="xtra"/><references/>
-	[[Category: ~~Enterobacteria phage t4~~]]	+	[[Category: Bpt4]]
	[[Category: Lysozyme]]		[[Category: Lysozyme]]
	[[Category: Baase, W A.]]		[[Category: Baase, W A.]]