1gbf - Revision history

OCA at 11:20, 27 March 2024

OCA — Wed, 27 Mar 2024 11:20:46 GMT

←Older revision		Revision as of 11:20, 27 March 2024
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	<StructureSection load='1gbf' size='340' side='right'caption='[[1gbf]], [[Resolution\|resolution]] 2.15Å' scene=''>		<StructureSection load='1gbf' size='340' side='right'caption='[[1gbf]], [[Resolution\|resolution]] 2.15Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1gbf]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GBF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GBF FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1gbf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lysobacter_enzymogenes Lysobacter enzymogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GBF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GBF FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.15Å</td></tr>
-	<tr id='~~NonStdRes~~'><td class="sblockLbl"><b>[[~~Non-Standard_Residue~~\|~~NonStd Res~~:]]</b></td><td class="sblockDat"><scene name='pdbligand=B2A:ALANINE+BORONIC+ACID'>B2A</scene>, <scene name='pdbligand=MSU:SUCCINIC+ACID+MONOMETHYL+ESTER'>MSU</scene><~~/td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=B2A:ALANINE+BORONIC+ACID'>B2A</scene>, <scene name='pdbligand=MSU:SUCCINIC+ACID+MONOMETHYL+ESTER'>MSU</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b></td><td class="sblockDat"><span class='plainlinks~~'>~~[https://en.wikipedia.org/wiki/Alpha-lytic_endopeptidase Alpha-lytic endopeptidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.12 3.4.21.12]~~ </~~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=1gbf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gbf OCA], [https://pdbe.org/1gbf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gbf RCSB], [https://www.ebi.ac.uk/pdbsum/1gbf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gbf 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=1gbf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gbf OCA], [https://pdbe.org/1gbf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gbf RCSB], [https://www.ebi.ac.uk/pdbsum/1gbf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gbf ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/PRLA_LYSEN PRLA_LYSEN]
	== 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=1gbf 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=1gbf ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Gly216 in the active site of the broadly specific MA190 mutant of alpha-lytic protease has been found to be remarkably tolerant of amino acid substitutions. Side-chains as large as Trp can be accommodated within the substrate-binding pocket without abolishing catalysis, and have major effects upon the substrate specificity of the enzyme. Kinetic characterization of eleven enzymatically active mutants against a panel of eight substrates clearly revealed the functional consequences of the substitutions at position 216. To understand better the structural basis for their altered specificity, the GA216 + MA190 and GL216 + MA190 mutants have been crystallized both with and without a representative series of peptide boronic acid transition-state analog inhibitors. An empirical description and non-parametric statistical analysis of structural variation among these enzyme: inhibitor complexes is presented. The roles of active site plasticity and dynamics in alpha-lytic protease function and substrate preference are also addressed. The results strongly suggest that substrate specificity determination in alpha-lytic protease is a distributed property of the active site and substrate molecule.
-
-	Kinetic and structural characterization of mutations of glycine 216 in alpha-lytic protease: a new target for engineering substrate specificity.,Mace JE, Agard DA J Mol Biol. 1995 Dec 8;254(4):720-36. PMID:7500345<ref>PMID:7500345</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1gbf" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Alpha-lytic protease 3D structures\|Alpha-lytic protease 3D structures]]		*[[Alpha-lytic protease 3D structures\|Alpha-lytic protease 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Alpha-lytic endopeptidase]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Agard, D A~~]]	+	[[Category: Lysobacter enzymogenes]]
-	[[Category: ~~Mace, J E~~]]	+	[[Category: Agard DA]]
-	[[Category: ~~Active-site mutation]]~~	+	[[Category: Mace JE]]
-	~~[[Category: Hydrolase-hydrolase inhibitor complex]]~~	+
-	~~[[Category: Serine proteinase~~]]	+

OCA at 11:00, 31 March 2021

OCA — Wed, 31 Mar 2021 11:00:12 GMT

←Older revision		Revision as of 11:00, 31 March 2021
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	<StructureSection load='1gbf' size='340' side='right'caption='[[1gbf]], [[Resolution\|resolution]] 2.15Å' scene=''>		<StructureSection load='1gbf' size='340' side='right'caption='[[1gbf]], [[Resolution\|resolution]] 2.15Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1gbf]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GBF OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1GBF FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1gbf]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GBF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GBF FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=B2A:ALANINE+BORONIC+ACID'>B2A</scene>, <scene name='pdbligand=MSU:SUCCINIC+ACID+MONOMETHYL+ESTER'>MSU</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=B2A:ALANINE+BORONIC+ACID'>B2A</scene>, <scene name='pdbligand=MSU:SUCCINIC+ACID+MONOMETHYL+ESTER'>MSU</scene></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Alpha-lytic_endopeptidase Alpha-lytic endopeptidase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.12 3.4.21.12] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Alpha-lytic_endopeptidase Alpha-lytic endopeptidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.12 3.4.21.12] </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=1gbf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gbf OCA], [~~http~~://pdbe.org/1gbf PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1gbf RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1gbf PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1gbf 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=1gbf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gbf OCA], [https://pdbe.org/1gbf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gbf RCSB], [https://www.ebi.ac.uk/pdbsum/1gbf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gbf ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==

OCA at 08:30, 26 June 2019

OCA — Wed, 26 Jun 2019 08:30:16 GMT

←Older revision		Revision as of 08:30, 26 June 2019
Line 1:		Line 1:

	==ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA AND GLY 216 REPLACED BY LEU COMPLEX WITH METHOXYSUCCINYL-ALA-ALA-PRO-ALANINE BORONIC ACID==		==ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA AND GLY 216 REPLACED BY LEU COMPLEX WITH METHOXYSUCCINYL-ALA-ALA-PRO-ALANINE BORONIC ACID==
-	<StructureSection load='1gbf' size='340' side='right' caption='[[1gbf]], [[Resolution\|resolution]] 2.15Å' scene=''>	+	<StructureSection load='1gbf' size='340' side='right'caption='[[1gbf]], [[Resolution\|resolution]] 2.15Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1gbf]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GBF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GBF FirstGlance]. <br>		<table><tr><td colspan='2'>[[1gbf]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GBF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GBF FirstGlance]. <br>
Line 13:		Line 13:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gb/1gbf_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gb/1gbf_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 30:		Line 30:

	==See Also==		==See Also==
-	*[[Alpha-lytic protease\|Alpha-lytic protease]]	+	*[[Alpha-lytic protease 3D structures\|Alpha-lytic protease 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 36:		Line 36:
	</StructureSection>		</StructureSection>
	[[Category: Alpha-lytic endopeptidase]]		[[Category: Alpha-lytic endopeptidase]]
		+	[[Category: Large Structures]]
	[[Category: Agard, D A]]		[[Category: Agard, D A]]
	[[Category: Mace, J E]]		[[Category: Mace, J E]]

OCA at 04:32, 21 September 2017

OCA — Thu, 21 Sep 2017 04:32:30 GMT

←Older revision		Revision as of 04:32, 21 September 2017
Line 1:		Line 1:
		+
	==ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA AND GLY 216 REPLACED BY LEU COMPLEX WITH METHOXYSUCCINYL-ALA-ALA-PRO-ALANINE BORONIC ACID==		==ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA AND GLY 216 REPLACED BY LEU COMPLEX WITH METHOXYSUCCINYL-ALA-ALA-PRO-ALANINE BORONIC ACID==
	<StructureSection load='1gbf' size='340' side='right' caption='[[1gbf]], [[Resolution\|resolution]] 2.15Å' scene=''>		<StructureSection load='1gbf' size='340' side='right' caption='[[1gbf]], [[Resolution\|resolution]] 2.15Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1gbf]] is a 2 chain structure ~~with sequence from [http://en.wikipedia.org/wiki/Atcc_29487 Atcc 29487]~~. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GBF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GBF FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1gbf]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GBF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GBF FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=B2A:ALANINE+BORONIC+ACID'>B2A</scene>, <scene name='pdbligand=MSU:SUCCINIC+ACID+MONOMETHYL+ESTER'>MSU</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=B2A:ALANINE+BORONIC+ACID'>B2A</scene>, <scene name='pdbligand=MSU:SUCCINIC+ACID+MONOMETHYL+ESTER'>MSU</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ALPHA-LYTIC PROTEASE PREPROENZ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=69 ATCC 29487])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha-lytic_endopeptidase Alpha-lytic endopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.12 3.4.21.12] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha-lytic_endopeptidase Alpha-lytic endopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.12 3.4.21.12] </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=1gbf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gbf OCA], [http://pdbe.org/1gbf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1gbf RCSB], [http://www.ebi.ac.uk/pdbsum/1gbf 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=1gbf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gbf OCA], [http://pdbe.org/1gbf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1gbf RCSB], [http://www.ebi.ac.uk/pdbsum/1gbf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1gbf ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
Line 17:		Line 17:
	<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=1gbf ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 36:		Line 36:
	</StructureSection>		</StructureSection>
	[[Category: Alpha-lytic endopeptidase]]		[[Category: Alpha-lytic endopeptidase]]
-	[[Category: Atcc 29487]]
	[[Category: Agard, D A]]		[[Category: Agard, D A]]
	[[Category: Mace, J E]]		[[Category: Mace, J E]]

OCA at 00:02, 12 September 2015

OCA — Sat, 12 Sep 2015 00:02:16 GMT

←Older revision		Revision as of 00:02, 12 September 2015
Line 2:		Line 2:
	<StructureSection load='1gbf' size='340' side='right' caption='[[1gbf]], [[Resolution\|resolution]] 2.15Å' scene=''>		<StructureSection load='1gbf' size='340' side='right' caption='[[1gbf]], [[Resolution\|resolution]] 2.15Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1gbf]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Lysobacter_enzymogenes Lysobacter enzymogenes~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GBF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GBF FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1gbf]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_29487 Atcc 29487]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GBF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GBF FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=B2A:ALANINE+BORONIC+ACID'>B2A</scene>, <scene name='pdbligand=MSU:SUCCINIC+ACID+MONOMETHYL+ESTER'>MSU</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=B2A:ALANINE+BORONIC+ACID'>B2A</scene>, <scene name='pdbligand=MSU:SUCCINIC+ACID+MONOMETHYL+ESTER'>MSU</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ALPHA-LYTIC PROTEASE PREPROENZ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=69 ~~Lysobacter enzymogenes~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ALPHA-LYTIC PROTEASE PREPROENZ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=69 ATCC 29487])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha-lytic_endopeptidase Alpha-lytic endopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.12 3.4.21.12] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha-lytic_endopeptidase Alpha-lytic endopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.12 3.4.21.12] </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=1gbf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gbf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1gbf RCSB], [http://www.ebi.ac.uk/pdbsum/1gbf 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=1gbf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gbf OCA], [http://pdbe.org/1gbf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1gbf RCSB], [http://www.ebi.ac.uk/pdbsum/1gbf PDBsum]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
Line 27:		Line 27:
	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 1gbf" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 35:		Line 36:
	</StructureSection>		</StructureSection>
	[[Category: Alpha-lytic endopeptidase]]		[[Category: Alpha-lytic endopeptidase]]
-	[[Category: ~~Lysobacter enzymogenes~~]]	+	[[Category: Atcc 29487]]
	[[Category: Agard, D A]]		[[Category: Agard, D A]]
	[[Category: Mace, J E]]		[[Category: Mace, J E]]

OCA at 22:12, 22 December 2014

OCA — Mon, 22 Dec 2014 22:12:05 GMT

OCA at 10:25, 3 October 2014

OCA — Fri, 03 Oct 2014 10:25:55 GMT

←Older revision		Revision as of 10:25, 3 October 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_1gbf\| PDB=1gbf \| SCENE= }}~~	+	==ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA AND GLY 216 REPLACED BY LEU COMPLEX WITH METHOXYSUCCINYL-ALA-ALA-PRO-ALANINE BORONIC ACID==
-	===ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA AND GLY 216 REPLACED BY LEU COMPLEX WITH METHOXYSUCCINYL-ALA-ALA-PRO-ALANINE BORONIC ACID===	+	<StructureSection load='1gbf' size='340' side='right' caption='[[1gbf]], [[Resolution\|resolution]] 2.15Å' scene=''>
-	~~{{ABSTRACT_PUBMED_7500345}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1gbf]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lysobacter_enzymogenes Lysobacter enzymogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GBF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GBF FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=B2A:ALANINE+BORONIC+ACID'>B2A</scene>, <scene name='pdbligand=MSU:SUCCINIC+ACID+MONOMETHYL+ESTER'>MSU</scene></td></tr>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ALPHA-LYTIC PROTEASE PREPROENZ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=69 Lysobacter enzymogenes])</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha-lytic_endopeptidase Alpha-lytic endopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.12 3.4.21.12] </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=1gbf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gbf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1gbf RCSB], [http://www.ebi.ac.uk/pdbsum/1gbf 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/gb/1gbf_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 ==
		+	Gly216 in the active site of the broadly specific MA190 mutant of alpha-lytic protease has been found to be remarkably tolerant of amino acid substitutions. Side-chains as large as Trp can be accommodated within the substrate-binding pocket without abolishing catalysis, and have major effects upon the substrate specificity of the enzyme. Kinetic characterization of eleven enzymatically active mutants against a panel of eight substrates clearly revealed the functional consequences of the substitutions at position 216. To understand better the structural basis for their altered specificity, the GA216 + MA190 and GL216 + MA190 mutants have been crystallized both with and without a representative series of peptide boronic acid transition-state analog inhibitors. An empirical description and non-parametric statistical analysis of structural variation among these enzyme: inhibitor complexes is presented. The roles of active site plasticity and dynamics in alpha-lytic protease function and substrate preference are also addressed. The results strongly suggest that substrate specificity determination in alpha-lytic protease is a distributed property of the active site and substrate molecule.

-	~~==About this Structure==~~	+	Kinetic and structural characterization of mutations of glycine 216 in alpha-lytic protease: a new target for engineering substrate specificity.,Mace JE, Agard DA J Mol Biol. 1995 Dec 8;254(4):720-36. PMID:7500345<ref>PMID:7500345</ref>
-	~~[[1gbf]] is a 2 chain structure with sequence from [http~~:~~//en~~.~~wikipedia~~.~~org/wiki/Lysobacter_enzymogenes Lysobacter enzymogenes]~~. ~~Full crystallographic information is available from [http~~://~~oca~~.~~weizmann~~.ac.il/~~oca-bin/ocashort?id=1GBF OCA].~~	+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

	==See Also==		==See Also==
	*[[Alpha-lytic protease\|Alpha-lytic protease]]		*[[Alpha-lytic protease\|Alpha-lytic protease]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:007500345</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Alpha-lytic endopeptidase]]		[[Category: Alpha-lytic endopeptidase]]
	[[Category: Lysobacter enzymogenes]]		[[Category: Lysobacter enzymogenes]]

OCA at 10:38, 16 April 2014

OCA — Wed, 16 Apr 2014 10:38:18 GMT

←Older revision		Revision as of 10:38, 16 April 2014
Line 1:		Line 1:
-	[[Image:1gbf.png\|left\|200px]]
-
-	<!--
-	The line below this paragraph, containing "STRUCTURE_1gbf", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_1gbf\| PDB=1gbf \| SCENE= }}		{{STRUCTURE_1gbf\| PDB=1gbf \| SCENE= }}
-
	===ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA AND GLY 216 REPLACED BY LEU COMPLEX WITH METHOXYSUCCINYL-ALA-ALA-PRO-ALANINE BORONIC ACID===		===ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA AND GLY 216 REPLACED BY LEU COMPLEX WITH METHOXYSUCCINYL-ALA-ALA-PRO-ALANINE BORONIC ACID===
-
-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_7500345}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 7500345 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_7500345}}		{{ABSTRACT_PUBMED_7500345}}

	==About this Structure==		==About this Structure==
	[[1gbf]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lysobacter_enzymogenes Lysobacter enzymogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GBF OCA].		[[1gbf]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lysobacter_enzymogenes Lysobacter enzymogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GBF OCA].
		+
		+	==See Also==
		+	*[[Alpha-lytic protease\|Alpha-lytic protease]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:007500345</ref><references group="xtra"/>	+	<ref group="xtra">PMID:007500345</ref><references group="xtra"/><references/>
	[[Category: Alpha-lytic endopeptidase]]		[[Category: Alpha-lytic endopeptidase]]
	[[Category: Lysobacter enzymogenes]]		[[Category: Lysobacter enzymogenes]]

OCA: Protected "1gbf" [edit=sysop:move=sysop]

OCA — Wed, 27 Jul 2011 04:49:54 GMT

Protected "1gbf" [edit=sysop:move=sysop]

←Older revision

Revision as of 04:49, 27 July 2011

OCA at 04:49, 27 July 2011

OCA — Wed, 27 Jul 2011 04:49:53 GMT

←Older revision		Revision as of 04:49, 27 July 2011
Line 1:		Line 1:
-	{{Seed}}
	[[Image:1gbf.png\|left\|200px]]		[[Image:1gbf.png\|left\|200px]]

Line 20:		Line 19:

	==About this Structure==		==About this Structure==
-	~~1GBF~~ is a 2 ~~chains~~ structure ~~of sequences~~ from [http://en.wikipedia.org/wiki/Lysobacter_enzymogenes Lysobacter enzymogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GBF OCA].	+	[[1gbf]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lysobacter_enzymogenes Lysobacter enzymogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GBF OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~7500345~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:007500345</ref><references group="xtra"/>
	[[Category: Alpha-lytic endopeptidase]]		[[Category: Alpha-lytic endopeptidase]]
	[[Category: Lysobacter enzymogenes]]		[[Category: Lysobacter enzymogenes]]
Line 29:		Line 28:
	[[Category: Mace, J E.]]		[[Category: Mace, J E.]]
	[[Category: Active-site mutation]]		[[Category: Active-site mutation]]
-	[[Category: ~~Inhibitor~~ complex]]	+	[[Category: Hydrolase-hydrolase inhibitor complex]]
-		+	[[Category: Serine proteinase]]
-	~~''Page seeded by~~ [~~http~~:~~//oca.weizmann.ac.il/oca OCA~~ ] ~~on Wed Feb 18 07:41:14 2009''~~	+

←Older revision		Revision as of 22:12, 22 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1gbf]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lysobacter_enzymogenes Lysobacter enzymogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GBF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GBF FirstGlance]. <br>		<table><tr><td colspan='2'>[[1gbf]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lysobacter_enzymogenes Lysobacter enzymogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GBF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GBF FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=B2A:ALANINE+BORONIC+ACID'>B2A</scene>, <scene name='pdbligand=MSU:SUCCINIC+ACID+MONOMETHYL+ESTER'>MSU</scene></td></tr>	+	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=B2A:ALANINE+BORONIC+ACID'>B2A</scene>, <scene name='pdbligand=MSU:SUCCINIC+ACID+MONOMETHYL+ESTER'>MSU</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ALPHA-LYTIC PROTEASE PREPROENZ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=69 Lysobacter enzymogenes])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ALPHA-LYTIC PROTEASE PREPROENZ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=69 Lysobacter enzymogenes])</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha-lytic_endopeptidase Alpha-lytic endopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.12 3.4.21.12] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha-lytic_endopeptidase Alpha-lytic endopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.12 3.4.21.12] </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=1gbf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gbf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1gbf RCSB], [http://www.ebi.ac.uk/pdbsum/1gbf 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=1gbf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gbf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1gbf RCSB], [http://www.ebi.ac.uk/pdbsum/1gbf 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 36:		Line 36:
	[[Category: Alpha-lytic endopeptidase]]		[[Category: Alpha-lytic endopeptidase]]
	[[Category: Lysobacter enzymogenes]]		[[Category: Lysobacter enzymogenes]]
-	[[Category: Agard, D A.]]	+	[[Category: Agard, D A]]
-	[[Category: Mace, J E.]]	+	[[Category: Mace, J E]]
	[[Category: Active-site mutation]]		[[Category: Active-site mutation]]
	[[Category: Hydrolase-hydrolase inhibitor complex]]		[[Category: Hydrolase-hydrolase inhibitor complex]]
	[[Category: Serine proteinase]]		[[Category: Serine proteinase]]